# ent

id: cord-000588-3wok0n21
type: ORG
entity:
  the European Organization for Research and Treatment of Cancer Invasive Fungal Infections Cooperative Group


id: cord-002395-goil7gjr
type: PROTEIN
entity:
  Stokes radius cytochrome c 17 Å bovine erythrocyte carbonic anhydrase 23 9 Å bovine serum albumin 35 5 Å yeast alcohol dehydrogenase 45 5 Å b amylase 51 Å E coli bgalactosidase 69 Å


id: cord-002395-goil7gjr
type: CHEMICAL
entity:
  N terminal SNARE region of SNAP25 and syntaxin 1a Impact of polymorphisms in the DC SIGNR neck domain


id: cord-002372-ody77u5n
type: PROTEIN
entity:
  type II transmembrane proteins SIGN R1 325 amino acids SIGN R3 237 amino acids SIGN R4 208 amino acids


id: cord-002058-rppsmirp
type: PROTEIN
entity:
  M bovis BCG chaperone protein DnaK DnaK 60 kDa chaperonin 1 Cpn60 1 glyceraldehyde 3 phosphate dehydrogenase GAPDH


id: cord-002058-rppsmirp
type: PROTEIN
entity:
  Helicobacter pylori Cpn60 1 60 kDa chaperonin 1 DC dendritic cell DC SIGN CD209 dendritic cell specific intercellular adhesion molecule 3


id: cord-021527-1etvgoxc
type: DISEASE
entity:
  carcinoma hemangioma histiocytoma leiomyosarcoma lymphoma myxosarcoma neurofibrosarcoma perianal gland adenocarcinoma sebaceous gland adenocarcinoma


id: cord-265600-lnik974k
type: DISEASE
entity:
  human immunodeficiency virus type 1 HIV 1 transmission Dendritic cell specific intercellular adhesion molecule 3 grabbing


id: cord-268902-npug5c8p
type: PROTEIN
entity:
  hepatocyte asialoglycoprotein receptor Human mannose binding protein carbohydrate recognition domain


id: cord-268902-npug5c8p
type: GGP
entity:
  mannose 6 phosphate receptor Herpes simplex virus glycoprotein D acquires mannose 6 phosphate residues


id: cord-022575-ybj6lwdb
type: DNA
entity:
  dog and cat The normal ear Diagnostic imaging of the canine and feline ear Imaging techniques in the diagnosis of middle ear disease Microbial flora and antimicrobial susceptibility patterns of isolated pathogens


id: cord-022575-ybj6lwdb
type: CELL_LINE
entity:
  cat with squamous cell carcinoma The cranial and nasal cavities canine and feline Results of magnetic resonance imaging in dogs with vestibular disorders 85 cases 1996 1999 Results of surgery in cats with ceruminous gland adenocarcinoma Clinical neurology in small animals localization diagnosis and treatment International Veterinary Information Service A comparison of radiographic versus surgical diagnosis of otitis media Radiographic and computed tomographic evaluation of otitis media Meningeal enhancement on magnetic resonance imaging in 15 dogs and 3 cats Feline vestibular disorders Part I anatomy


id: cord-018864-c1r2n17o
type: DISEASE
entity:
  human immunodeficiency virus type 1 Detection of HIV1 RNA and p24 antigen in HIV1 infected human liver


id: cord-017258-5mzr5s22
type: WORK_OF_ART
entity:
  Langerhans cells Engagement of BDCA 2 blocks TRAILmediated cytotoxic activity of plasmacytoid dendritic cells


id: cord-017258-5mzr5s22
type: DISEASE
entity:
  Kawasaki disease autoimmune dermatomyositis vasculitis neuropathy myasthenia gravis pemphigus vulgaris


id: cord-267234-waz0k0ms
type: GGP
entity:
  Comp Immunol DOI 10 1016 j dci 2015 01 004 sha ab7c5bbcff6f13e19d69ea09e776cb830dedaf90 doc_id 267234 cord_uid waz0k0ms


id: cord-021453-vf8xbaug
type: ORG
entity:
  Subpart A Specifications for the Humane Handling Care Treatment and Transportation of Dogs and Cats of Part 3 Standards of Subchapter A Particular


id: cord-021453-vf8xbaug
type: ORG
entity:
  the Association for Assessment and Accreditation of Laboratory Animal Care International AAALAC International


id: cord-021453-vf8xbaug
type: CHEMICAL
entity:
  b978 012263951 7 50014 4 sha f324d188da605b12c1b89a3d83688c0203d0e950 doc_id 21453 cord_uid vf8xbaug nan status


id: cord-021453-vf8xbaug
type: DISEASE
entity:
  rodenticide intoxication coagulopathies heartworm disease pulmonary thromboembolism ruptured aneurysm


id: cord-021453-vf8xbaug
type: DISEASE
entity:
  thoracic radiography pulmonary artery and right heart enlargement electrocardiography right heart enlargement


id: cord-021453-vf8xbaug
type: DISEASE
entity:
  malignant solid carcinomas tubular adenocarcinomas papillary adenocarcinomas anaplastic carcinomas sarcomas


id: cord-021453-vf8xbaug
type: DISEASE
entity:
  deafness cataracts glaucoma microphthalmos optic nerve hypoplasia retinal dysplasia tapetal hypoplasia


id: cord-287799-ridm3qd7
type: CL
entity:
  enteroinvasive Escherichia coli EIEC Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356 Synergistic


id: cord-287799-ridm3qd7
type: DISEASE
entity:
  Consensus Von Eichel Streiber Carbohydrate binding sites 29 pI was predicted with Protparam Expasy Consensuses


id: cord-022520-ebj51v9o
type: CHEMICAL
entity:
  b978 012263951 7 50016 8 sha e87d436d32199acf0b99a4ebbabf654f76af2e44 doc_id 22520 cord_uid ebj51v9o nan Ferrets Mustela


id: cord-300272-95o8yd7h
type: ORG
entity:
  the Interaction of Ebola Virus Glycoprotein with DC SIGN Dendritic Cell Specific Intercellular Adhesion Molecule 3


id: cord-300272-95o8yd7h
type: ORG
entity:
  Sulfate Proteoglycans for Attachment to Target Cells C Type Lectin Receptors in Host Defense Against Bacterial Pathogens Dendritic


id: cord-342936-43u7afl3
type: DISEASE
entity:
  human immunodeficiency virus HIVHIV 1 and hepatitis C virus HCV closely correlates for carbohydrate binding


id: cord-344124-1ztyj0z4
type: DISEASE
entity:
  herpes simplex virus type 1 37 the human cytomegalovirus 38 Ebola virus 39 the SARS coronavirus 40 41 the human T cell leukemia virus type 1 42 43 and arboviruses belonging to the flavivirus genus dengue


id: cord-333655-lylt7qld
type: PROTEIN
entity:
  ethanolamine PO 4 6Mana1 2Mana1 6Mana1 4GlcNa1 6myo inositol 1 PO 4 lipid Differential derivatization


id: cord-333655-lylt7qld
type: DISEASE
entity:
  human immunodeficiency virus type 1 HIV 1 and human langerin a C type lectin mainly expressed on Langerhans cells de Witte


id: cord-333655-lylt7qld
type: DISEASE
entity:
  human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization The alpha 1 2 mannosidase I inhibitor 1 deoxymannojirimycin


id: cord-333655-lylt7qld
type: DISEASE
entity:
  HIV 2 envelope glycoprotein Differential N linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins


id: cord-333655-lylt7qld
type: DISEASE
entity:
  herpes simplex virus type 1 The multiple facets of HIV attachment to dendritic cell lectins Platelet activation


id: cord-333655-lylt7qld
type: DISEASE
entity:
  HIV on dendritic cell subsets Immunodeficiency virus uptake turnover and 2 phase transfer in human dendritic cells The M GP 5 glycoprotein complex of porcine reproductive and respiratory syndrome


id: cord-275863-qos9vu3r
type: DNA
entity:
  jir173 sha 3062cebd70447841d68c48fe83f0eb51b07a761d doc_id 275863 cord_uid qos9vu3r Dengue virus receptors


id: cord-275863-qos9vu3r
type: PROTEIN
entity:
  glycan antigen Lewis x A dendritic cell specific intercellular adhesion molecule 3 grabbing nonintegrin DC SIGN related protein


id: cord-023367-ujflw19b
type: DISEASE
entity:
  intestinal malabsorption electrolyte loss metabolic acidosis hypoglycemia hyponatremia hypochloremia hyperkalemia


id: cord-022555-a7ie82fs
type: PROTEIN
entity:
  Cat DOI 10 1016 b978 1 4377 0660 4 00023 5 sha 43302f8eebca5d76d6388fe2286ead361a68209a doc_id 22555 cord_uid a7ie82fs nan


id: cord-022555-a7ie82fs
type: CELL_TYPE
entity:
  intestinal mast cell tumors adenomatous polyps eosinophilic sclerosing fibroplasia gastrointestinal stromal tumors leiomyosarcoma and hemangiosarcoma Mast cell tumors MCT


id: cord-022555-a7ie82fs
type: DNA
entity:
  dog and the other causes of portal hypertension Budd Chiari syndrome heartworm caval syndrome pulmonary hypertension


id: cord-022555-a7ie82fs
type: DNA
entity:
  dog and cat Pharmacokinetics and suggested oral dosing regimen of cisapride a study in healthy cats Intussusception


id: cord-022555-a7ie82fs
type: CELL_LINE
entity:
  cat Feline exocrine pancreatic insufficiency 16 cases Pancreatitis associated with a feline herpesvirus infection Pancreatic pseudocysts


id: cord-022555-a7ie82fs
type: GGP
entity:
  Clostridium piliforme Tyzzer s disease 71 and Anaerobiospirillum sp 36 Specific diagnosis of these and other


id: cord-021555-rrverrsj
type: ORG
entity:
  Current Veterinary Therapy Food Animal Practice Livestock Handling Guide Management Practices that Reduce Livestock Bruises and Injuries


id: cord-021555-rrverrsj
type: WORK_OF_ART
entity:
  Animal Models of Human Disease Bibliography of Naturally Occurring Models of Human Disease Postpartum


id: cord-021555-rrverrsj
type: DISEASE
entity:
  abscesses tetanus selenium vitamin E deficiencies copper deficiency strawberry foot rot bluetongue virus infection


id: cord-267671-ys43n672
type: PROTEIN
entity:
  S2 I1 I2 I3 I4 I5 I6 C1 C2 L1 L2 L3 E1 S1 S2 I1 I2 I3 I4 I5 I6 C1 C2 L1 L2 L3 E1 S1 S2 I1 I2 I3 I4 I5 I6 C1 C2 L1 L2 L3 E1 S1 S2 I1 I2 I3 I4 I5 I6 C1 C2 L1 L2


id: cord-267671-ys43n672
type: CELL_TYPE
entity:
  lung skeletal muscle myocardium kidneys nerves and adrenal glands The histologic hallmark is perivascular granulomatosis


id: cord-267671-ys43n672
type: CELL_TYPE
entity:
  glycogen positive intracytoplasmic inclusions elementary bodies C trachomatis causes ocular and urogenital disease


id: cord-267671-ys43n672
type: CELL_LINE
entity:
  transmissible murine colonic hyperplasia Mouse hepatitis virus infection intestine mouse Mouse hepatitis virus infection liver mouse Murine rotavirus infection intestine mouse


id: cord-267671-ys43n672
type: GGP
entity:
  I1 I2 I3 I4 I5 I6 C1 C2 L1 L2 L3 E1 S1 S2 I1 I2 I3 I4 I5 I6 C1 C2 L1 L2 L3 E1 S1 S2 I1 I2 I3 I4 I5 I6 C1 C2 L1 L2 L3 E1 S1 S2 I1 I2 I3 I4 I5 I6 C1 C2 L1


id: cord-267671-ys43n672
type: CL
entity:
  lymphopoietic and hematopoietic neoplasia belong to the family Retroviridae type C oncornaviruses and contain RNA


id: cord-267671-ys43n672
type: DISEASE
entity:
  Komarek 2007 fallopian tube 3 uterine horn 4 endometrium 5 cervix 6 vagina 7 vaginal vestibulum 8 clitoris 9 clitoral gland 10 urethra 11 bladder 12 medial ligament


id: cord-026031-hnf5vayd
type: CELL_TYPE
entity:
  malignant hemangiosarcoma lymphoma mast cell tumor malignant fibrous histiocytoma leiomyosarcoma fibrosarcoma


id: cord-026031-hnf5vayd
type: GGP
entity:
  blockers e g propranolol Cardiac glycosides e g digoxin Urethral obstruction Ruptured bladder Anuric


id: cord-026031-hnf5vayd
type: GGP
entity:
  Angiotensin converting enzyme inhibitors e g enalapril Angiotensin receptor blockers e g losartan Cyclosporine


id: cord-026031-hnf5vayd
type: GGP
entity:
  steroids e g prednisolone methylprednisolone sodium succinate triamcinolone Depending on the severity of the patient s condition consider monitoring using the Rule of Twenty Administer antiemetics and gastroprotectant drugs to treat nausea vomiting and hematemesis Give the patient broad spectrum antibiotics ampicillin


id: cord-026031-hnf5vayd
type: GGP
entity:
  allethrin decamethrin tralomethrin fenpropanthrin pallethrin sumethrin permethrin tetramethrin cyfluthrin


id: cord-026031-hnf5vayd
type: GGP
entity:
  warfarin 0 06 0 09 mg kg day Monitoring therapy based on prothrombin time and the international normalized ratio INR 2 0 4 0


id: cord-026031-hnf5vayd
type: WORK_OF_ART
entity:
  Treatment Treatment of onion chive and garlic toxicity includes administration of intravenous fluid diuresis and induction of


id: cord-026031-hnf5vayd
type: DISEASE
entity:
  pyometra gastrointestinal obstruction intraluminal gastrointestinal foreign body dilated bile duct or gallbladder mucocele


id: cord-026031-hnf5vayd
type: DISEASE
entity:
  hypotension shock coagulopathies lethargy weakness muscle fasciculations lymphangitis rhabdomyolysis


id: cord-026031-hnf5vayd
type: DISEASE
entity:
  concomitant ligamentous or neurologic compromise Box 1 41 Immediately after the initial primary survey of a patient perform a more thorough examination including an orthopedic examination Multiple injuries


id: cord-026031-hnf5vayd
type: CHEMICAL
entity:
  NaCl 2 5 dextrose 150 200 5 0 45 NaCl 2 5 dextrose 100 150 5 0 45 NaCl 2 5 dextrose 100 0 0 45 NaCl 5 dextrose


id: cord-026031-hnf5vayd
type: DISEASE
entity:
  tremors nervousness polyphagia ataxia tachycardia muscle twitching incoordination visual disturbances


id: cord-026031-hnf5vayd
type: DISEASE
entity:
  vomiting ataxia hypersalivation agitation tremors hyperactivity hyperthermia hypoventilation coma seizures


id: cord-026031-hnf5vayd
type: DISEASE
entity:
  primary pulmonary parenchymal disease airway disease thoracic cage disorders congestive heart failure


id: cord-026031-hnf5vayd
type: DISEASE
entity:
  infectious peritonitis congestive heart failure chylothorax heartworm disease hemothorax hypoalbuminemia lung lobe torsions neoplasia diaphragmatic hernia


id: cord-026031-hnf5vayd
type: CHEMICAL
entity:
  Antihistamines loratadine diphenhydramine doxylamine clemastine meclizine dimenhydrinate chlorpheniramine cyclizine terfenadine hydroxyzine


id: cord-026031-hnf5vayd
type: DISEASE
entity:
  pleural hemorrhage gastrointestinal hemorrhage pericardial hemorrhage hematuria retroperitoneal hemorrhage hemarthrosis


id: cord-022526-j9kg00qf
type: PROTEIN
entity:
  interleukin 1 receptor associated kinase tumor necrosis factor receptor associated factor NFκB inducing kinase


id: cord-022526-j9kg00qf
type: PROTEIN
entity:
  haptoglobin transferrin ferritin ceruloplasmin coagulation factor VIII C serum amyloid A protein C reactive protein


id: cord-022526-j9kg00qf
type: PROTEIN
entity:
  alkaline phosphatase lactic dehydrogenase creatine kinase aspartate aminotransferase tumor necrosis heparin


id: cord-022526-j9kg00qf
type: GGP
entity:
  haptoglobin transferrin ferritin ceruloplasmin coagulation factor VIII C serum amyloid A protein C reactive protein α 1 acid glycoprotein


id: cord-022526-j9kg00qf
type: DISEASE
entity:
  abnormal occlusal contact and initiation of the cycle of irregular wear and abnormal contact Such changes progress to loss of alveolar bone gross periodontal sepsis


# bib

id: cord-000588-3wok0n21
title: Dectin-1 and DC-SIGN Polymorphisms Associated with Invasive Pulmonary Aspergillosis Infection
author: Sainz, Juan
date: 2012-02-27
txt: ./txt/cord-000588-3wok0n21.txt
cache: ./cache/cord-000588-3wok0n21.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3288082/
doi: 10.1371/journal.pone.0032273
summary:
  The present study was designed to investigate whether the presence of single nucleotide polymorphisms (SNPs) within DC-SIGN, Dectin-1, Dectin-2, CCL2 and CCR2 genes influence the risk of developing Invasive Pulmonary Aspergillosis (IPA). In addition, healthy individuals with this latter genotype showed a significantly decreased level of Dectin-1 mRNA expression compared to C-allele carriers, suggesting a role of the Dectin-1 (rs7309123) polymorphism in determining the levels of Dectin-1 and, consequently, the level of susceptibility to IPA infection. Based on these observations, the objective of the present study was to investigate the role of tagging and potentially functional single-nucleotide polymorphisms (SNPs) located within the DC-SIGN, Dectin-1, Dectin-2, MCP-1/CCL2 and CCR2 genes on IPA susceptibility. Of note is that two SNPs showing genetic interaction in this model were not significantly associated with an increased risk of IPA infection in the univariate analysis (CCR2 rs3918358 and Dectin-2 rs7134303 ).

abstract:
  The recognition of pathogen-derived structures by C-type lectins and the chemotactic activity mediated by the CCL2/CCR2 axis are critical steps in determining the host immune response to fungi. The present study was designed to investigate whether the presence of single nucleotide polymorphisms (SNPs) within DC-SIGN, Dectin-1, Dectin-2, CCL2 and CCR2 genes influence the risk of developing Invasive Pulmonary Aspergillosis (IPA). Twenty-seven SNPs were selected using a hybrid functional/tagging approach and genotyped in 182 haematological patients, fifty-seven of them diagnosed with proven or probable IPA according to the 2008 EORTC/MSG criteria. Association analysis revealed that carriers of the Dectin-1 (rs3901533 T/T) and Dectin-1 (rs7309123 G/G) genotypes and DC-SIGN (rs4804800 G), DC-SIGN (rs11465384 T), DC-SIGN (7248637 A) and DC-SIGN (7252229 C) alleles had a significantly increased risk of IPA infection (OR = 5.59 95%CI 1.37–22.77; OR = 4.91 95%CI 1.52–15.89; OR = 2.75 95%CI 1.27–5.95; OR = 2.70 95%CI 1.24–5.90; OR = 2.39 95%CI 1.09–5.22 and OR = 2.05 95%CI 1.00–4.22, respectively). There was also a significantly increased frequency of galactomannan positivity among patients carrying the Dectin-1 (rs3901533_T) allele and Dectin-1 (rs7309123_G/G) genotype. In addition, healthy individuals with this latter genotype showed a significantly decreased level of Dectin-1 mRNA expression compared to C-allele carriers, suggesting a role of the Dectin-1 (rs7309123) polymorphism in determining the levels of Dectin-1 and, consequently, the level of susceptibility to IPA infection. SNP-SNP interaction (epistasis) analysis revealed significant interactions models including SNPs in Dectin-1, Dectin-2, CCL2 and CCR2 genes, with synergistic genetic effects. Although these results need to be further validated in larger cohorts, they suggest that Dectin-1, DC-SIGN, Dectin-2, CCL2 and CCR2 genetic variants influence the risk of IPA infection and might be useful in developing a risk-adapted prophylaxis.


id: cord-002058-rppsmirp
title: Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG
author: Carroll, Maria V.
date: 2010-09-01
txt: ./txt/cord-002058-rppsmirp.txt
cache: ./cache/cord-002058-rppsmirp.txt
extension: .txt
mime: text/plain
url: https://link.springer.com/content/pdf/10.1007%2Fs13238-010-0101-3.pdf
doi: 10.1007/s13238-010-0101-3
summary:
  The novel ligands are chaperone protein DnaK, 60 kDa chaperonin-1 (Cpn60.1), glyceraldehyde-3 phosphate dehydrogenase (GAPDH) and lipoprotein lprG. bovis BCG can bind to dendritic-cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN/CD209) to promote entry into human dendritic cells (DCs) and alveolar macrophages Maeda et al., 2003; Tailleux et al., 2003; Pitarque et al., 2005; Appelmelk et al., 2008) . However, the form of this protein identified after capture by the affinity column was not glycosylated at this position, and it is therefore very unlikely that DC-SIGN binds to this ligand via its Ca 2+ -dependent lectin activity. bovis BCG lysate incubated with either 125 I-DC-SIGN or 125 I-DC-SIGNR revealed that DC-SIGN and DC-SIGNR both bind the same protein at around 27 kDa, which corresponds to lprG in our SDS-PAGE system, and is the only ligand detected by this method. DC-SIGN and DC-SIGNR binding to lprG can therefore still occur when the mycobacterial protein has been denatured by SDS-PAGE.

abstract:
  Dendritic-cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN; CD209) has an important role in mediating adherence of Mycobacteria species, including M. tuberculosis and M. bovis BCG to human dendritic cells and macrophages, in which these bacteria can survive intracellularly. DC-SIGN is a C-type lectin, and interactions with mycobacterial cells are believed to occur via mannosylated structures on the mycobacterial surface. Recent studies suggest more varied modes of binding to multiple mycobacterial ligands. Here we identify, by affinity chromatography and mass-spectrometry, four novel ligands of M. bovis BCG that bind to DC-SIGN. The novel ligands are chaperone protein DnaK, 60 kDa chaperonin-1 (Cpn60.1), glyceraldehyde-3 phosphate dehydrogenase (GAPDH) and lipoprotein lprG. Other published work strongly suggests that these are on the cell surface. Of these ligands, lprG appears to bind DC-SIGN via typical proteinglycan interactions, but DnaK and Cpn60.1 binding do not show evidence of carbohydrate-dependent interactions. LprG was also identified as a ligand for DC-SIGNR (L-SIGN; CD299) and the M. tuberculosis orthologue of lprG has been found previously to interact with human toll-like receptor 2. Collectively, these findings offer new targets for combating mycobacterial adhesion and within-host survival, and reinforce the role of DCSIGN as an important host ligand in mycobacterial infection.


id: cord-002372-ody77u5n
title: Animal lectins: potential receptors for ginseng polysaccharides
author: Loh, So Hee
date: 2015-12-17
txt: ./txt/cord-002372-ody77u5n.txt
cache: ./cache/cord-002372-ody77u5n.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5223067/
doi: 10.1016/j.jgr.2015.12.006
summary:
  Ginseng polysaccharides (GPs) are the responsible ingredient of ginseng in immunomodulation, and are classified as acidic and neutral GPs. Although GPs participate in various immune reactions including the stimulation of immune cells and production of cytokines, the precise function of GPs together with its potential receptor(s) and their signal transduction pathways have remained largely unknown. quinquefolius are mediated by PS with a molecular weight higher than 100 kDa. It was reported that acidic GPs promoted the production of cytotoxic cells against tumors and stimulated macrophages to produce helper types 1 and 2 (Th1 and Th2) cytokines [26, 27] . Because GPs were reported to significantly increase the viability of peritoneal macrophage cells [8] and ginseng was shown to inhibit degradation of long-lived proteins and to stimulate protein synthesis similar to polypeptide growth factors [41] , it was suggested that maintaining the cell viability under the condition of viral infection-induced stress might be an another alternative mechanism for the protective effects of GP.

abstract:
  Panax ginseng Meyer, belonging to the genus Panax of the family Araliaceae, is known for its human immune system-related effects, such as immune-boosting effects. Ginseng polysaccharides (GPs) are the responsible ingredient of ginseng in immunomodulation, and are classified as acidic and neutral GPs. Although GPs participate in various immune reactions including the stimulation of immune cells and production of cytokines, the precise function of GPs together with its potential receptor(s) and their signal transduction pathways have remained largely unknown. Animal lectins are carbohydrate-binding proteins that are highly specific for sugar moieties. Among many different biological functions in vivo, animal lectins especially play important roles in the immune system by recognizing carbohydrates that are found exclusively on pathogens or that are inaccessible on host cells. This review summarizes the immunological activities of GPs and the diverse roles of animal lectins in the immune system, suggesting the possibility of animal lectins as the potential receptor candidates of GPs and giving insights into the development of GPs as therapeutic biomaterials for many immunological diseases.


id: cord-002395-goil7gjr
author: dos Santos, Ália
date: 2016-12-22
txt: ./txt/cord-002395-goil7gjr.txt
cache: ./cache/cord-002395-goil7gjr.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5275740/
doi: 10.1002/pro.3083
summary:
  The results demonstrate that two features characterize repeat units which form more stable tetramers: a leucine reside in the first position of the heptad pattern of hydrophobic residues that pack on the inside of the coiled coil and an arginine residue on the surface of the coiled coil that forms a salt bridge with a glutamic acid residue in the same polypeptide chain. Gel filtration revealed that this version of the neck domain forms a stable tetramer at room temperature since it elutes at the same position as a natural fragment of the neck domain of DC-SIGNR containing seven repeat units, which has been characterized as a tetramer [ Fig. 3(A) ]. The studies reported here suggest that the presence of stabilizing residues at positions 6 and 15 of the repeat units allows for the formation of stable tetramers even for shorter versions of the neck domain present in some individuals, which result from common genetic polymorphisms in the human population.

title:
  Oligomerization domains in the glycan‐binding receptors DC‐SIGN and DC‐SIGNR: Sequence variation and stability differences

abstract:
  Human dendritic cell‐specific intercellular adhesion molecule‐1 grabbing nonintegrin, DC‐SIGN, and the sinusoidal endothelial cell receptor DC‐SIGNR or L‐SIGN, are closely related sugar‐binding receptors. DC‐SIGN acts both as a pathogen‐binding endocytic receptor and as a cell adhesion molecule, while DC‐SIGNR has only the pathogen‐binding function. In addition to differences in the sugar‐binding properties of the carbohydrate‐recognition domains in the two receptors, there are sequence differences in the adjacent neck domains, which are coiled‐coil tetramerization domains comprised largely of 23‐amino acid repeat units. A series of model polypeptides consisting of uniform repeat units have been characterized by gel filtration, differential scanning calorimetry and circular dichroism. The results demonstrate that two features characterize repeat units which form more stable tetramers: a leucine reside in the first position of the heptad pattern of hydrophobic residues that pack on the inside of the coiled coil and an arginine residue on the surface of the coiled coil that forms a salt bridge with a glutamic acid residue in the same polypeptide chain. In DC‐SIGNR from all primates, very stable repeat units predominate, so the carbohydrate‐recognition domains must be held relatively closely together. In contrast, stable repeat units are found only near the membrane in DC‐SIGN. The presence of residues that disrupt tetramer formation in repeat units near the carbohydrate‐recognition domains of DC‐SIGN would allow these domains to splay further apart. Thus, the neck domains of DC‐SIGN and DC‐SIGNR can contribute to the different functions of these receptors by presenting the sugar‐binding sites in different contexts.


id: cord-009669-bcdjwpd1
title: The multiple facets of HIV attachment to dendritic cell lectins
author: Tsegaye, Theodros Solomon
date: 2010-09-20
txt: ./txt/cord-009669-bcdjwpd1.txt
cache: ./cache/cord-009669-bcdjwpd1.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7162262/
doi: 10.1111/j.1462-5822.2010.01519.x
summary:
  Trans-infection was reported to depend on DC-SIGNmediated binding and cellular uptake of HIV into dendritic cells (Geijtenbeek et al., 2000; Kwon et al., 2002) , followed by intracellular transport of virions to sites of dendritic cell-T cell contact, termed infectious synapses (McDonald et al., 2003) (Fig. 1) . Finally, signalling via TLR8 and DC-SIGN was required for NFkB-dependent recruitment of the transcription factor pTEF-b to the viral promoter, and thus for the generation of full-length HIV transcripts in dendritic cells -a prerequisite for productive infection (Gringhuis et al., 2010) (Fig. 2) . Dendritic cell-mediated trans-enhancement of human immunodeficiency virus type 1 infectivity is independent of DC-SIGN The C-type lectin surface receptor DCIR acts as a new attachment factor for HIV-1 in dendritic cells and contributes to trans-and cis-infection pathways Functionally distinct transmission of human immunodeficiency virus type 1 mediated by immature and mature dendritic cells

abstract:
  Entry of enveloped viruses into host cells depends on the interactions of viral surface proteins with cell surface receptors. Many enveloped viruses maximize the efficiency of receptor engagement by first binding to attachment‐promoting factors, which concentrate virions on target cells and thus increase the likelihood of subsequent receptor engagement. Cellular lectins can recognize glycans on viral surface proteins and mediate viral uptake into immune cells for subsequent antigen presentation. Paradoxically, many viral and non‐viral pathogens target lectins to attach to immune cells and to subvert cellular functions to promote their spread. Thus, it has been proposed that attachment of HIV to the dendritic cell lectin DC‐SIGN enables the virus to hijack cellular transport processes to ensure its transmission to adjacent T cells. However, recent studies show that the consequences of viral capture by immune cell lectins can be diverse, and can entail negative and positive regulation of viral spread. Here, we will describe key concepts proposed for the role of lectins in HIV attachment to host cells, and we will discuss recent findings in this rapidly evolving area of research.


id: cord-017258-5mzr5s22
title: C-Type Lectin Receptors
author: Kanazawa, Nobuo
date: 2015-11-30
txt: ./txt/cord-017258-5mzr5s22.txt
cache: ./cache/cord-017258-5mzr5s22.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7121771/
doi: 10.1007/978-4-431-55855-2_17
summary:
  Similar to the killer lectin-like receptors whose genes are clustered in this complex, most of the CLRs induce activating or regulatory signal cascades in response to distinct pathogenor self-derived components, through the immunoreceptor tyrosine-based activating or inhibitory motif, respectively. They commonly consist of an N-terminal cysteine-rich domain and a fibronectin type II domain as well as eight or ten CTLDs. In contrast, the asialoglycoprotein receptor family (group II) contains type II transmembrane proteins with a single CTLD, such as DC-specific ICAM3-grabbing nonintegrin (DC-SIGN, CD209), dectin-1, dectin-2, DC immunoreceptor (DCIR), and macrophage-inducible C-type lectin (Mincle) [4, 5, 9, 33, 69] . Notably, expression of some receptors is specific and they can be markers for distinct DC subsets; langerin (CD207) on Langerhans cells (LCs) and blood DC antigen (BDCA)-2 (CD303) on plasmacytoid DCs (pDCs) [25, 99] .

abstract:
  C-type lectins, originally defined as proteins binding carbohydrates in a Ca(2+)-dependent manner, form a large family containing soluble and membrane-bound proteins. Among them, those expressed on phagocytes and working as pathogen pattern-recognition receptors were designated as C-type lectin receptors (CLRs), in accordance with Toll-like receptors (TLRs), NOD-like receptors (NLRs), and RIG-I–like receptors (RLRs). Most of the genes for CLRs are clustered in human chromosome 12 close to the natural killer gene complex. Similar to the killer lectin-like receptors whose genes are clustered in this complex, most of the CLRs induce activating or regulatory signal cascades in response to distinct pathogen- or self-derived components, through the immunoreceptor tyrosine-based activating or inhibitory motif, respectively. In this chapter, some representative CLRs are picked up and their structural features leading to the functional consequences are discussed, especially on the signaling cascades and pathogen interactions, including some impacts on cutaneous pathophysiology. These CLRs should provide targets to develop effective vaccination and therapeutics for distinct infectious and autoimmune/inflammatory diseases.


id: cord-018864-c1r2n17o
title: Attachment of human immunodeficiency virus to cells and its inhibition
author: Pöhlmann, Stefan
date: 2007
txt: ./txt/cord-018864-c1r2n17o.txt
cache: ./cache/cord-018864-c1r2n17o.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7123856/
doi: 10.1007/978-3-7643-7783-0_3
summary:
  In fact, the determinant role played by dendritic cells (DCs) in HIV-1 transmission might rely on specific interactions between gp120 and C-type lectins, of which the DC-specific intercellular adhesion molecule-3 (ICAM-3) grabbing nonintegrin (DC-SIGN) and DC-SIGNR (for DC-SIGN-related) are the best studied [10, 11]. In addition to its own virus-encoded envelope glycoproteins, the virus incorporates many different cellular proteins normally found on the cell surface (reviewed in [12] [13] [14] [15] The process of incorporation of host cell membrane proteins was found to be conserved among all tested HIV-1 subtypes and strains that were expanded in natural cellular reservoirs, such as mitogen-activated peripheral blood lymphocytes and human lymphoid tissue cultured ex vivo [27] [28] [29] [30] [31] [32] . Statin compounds reduce human immunodeficiency virus type 1 replication by preventing the interaction between virion-associated host intercellular adhesion molecule 1 and its natural cell surface ligand LFA-1 A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection

abstract:
  The entry of enveloped viruses involves virus adsorption followed by close apposition of the viral and plasma membranes. This multistep process is initiated by specific binding interactions between glycoproteins in the viral envelope and appropriate receptors on the cell surface. In the case of HIV-1, attachment of virions to the cell surface is attributed to a high affinity interaction between envelope spike glycoproteins (Env, composed of the surface protein gp120 and the transmembrane protein gp41) and a complex made of the primary CD4 receptor and a seven-transmembrane co-receptor (e.g., CXCR4 or CCR5) (reviewed in [1]). Then a chain of dynamic events take place that enable the viral nucleocapsid to penetrate within the target cell following the destabilization of membrane microenvironment and the formation of a fusion pore.


id: cord-021527-1etvgoxc
title: Ferrets
author: Ellis, Christine
date: 2009-05-15
txt: ./txt/cord-021527-1etvgoxc.txt
cache: ./cache/cord-021527-1etvgoxc.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7150118/
doi: 10.1016/b0-72-160422-6/50177-7
abstract: nan
summary:
  • Diagnosis is based on the medical history, the physical examination findings, and a complete diagnostic work-up that includes a CBC, reticulocyte count, serum biochemical analysis, whole-body radiographs, and bone marrow cytology if indicated. M Key Point Base a presumptive diagnosis of insulinoma on the history, clinical signs, and repeated evidence of hypoglycemia in the presence of normal or elevated blood insulin levels. Lymphosarcoma (lymphoma) is common in ferrets of all ages, and is similar in presentation to the disease in cats and dogs (see Chapter 27). • Differential diagnoses include the early stages of adrenal gland disease; however, hair loss on the body typically occurs as well when this condition is present. • Ferrets with congestive heart failure (CHF) may present with clinical signs that resemble symptoms associated with other disease entities, such as anorexia, ascites, coughing, dehydration, dyspnea, exercise intolerance, generalized weakness, hindlimb weakness, hypothermia, lethargy, tachypnea, and weight loss.


id: cord-021555-rrverrsj
title: Biology and Diseases of Ruminants: Sheep, Goats, and Cattle
author: Delano, Margaret L.
date: 2007-09-02
txt: ./txt/cord-021555-rrverrsj.txt
cache: ./cache/cord-021555-rrverrsj.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7150219/
doi: 10.1016/b978-012263951-7/50017-x
abstract: nan
summary:
  These references also provide information regarding vaccination products licensed for use in ruminants and typical herd and flock vaccination parasite control schedules ("Current Veterinary Therapy," 1986 , 1999 "Council report," 1994; "Large Animal Internal Medicine," 1996; Smith and Sherman, 1994) When designing a vaccination program during qualification of a source or at the research facility, it is important to evaluate the local disease incidence and the potential for exposure. Clinical signs in chronic cases in older animals, such as adult goats, include soft stools, weight loss, anorexia, depression, and severe diarrhea, sometimes with mucus and blood. This pathogen does present a complication due to the carrier status of some animals, the likelihood of herd outbreaks, the severity of disease in younger animals, and the morbidity, possible progression to uveitis, and time and treatment costs associated with infections.


id: cord-022203-t2f0vr1w
title: The pyrexic cat
author: Dowers, Kristy L
date: 2009-05-15
txt: ./txt/cord-022203-t2f0vr1w.txt
cache: ./cache/cord-022203-t2f0vr1w.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7155435/
doi: 10.1016/b978-0-7020-2488-7.50024-7
abstract: nan
summary:
  Clinical signs are often non-specific and include fever, anorexia and weight loss. Gastrointestinal signs are uncommon in cats compared to dogs, and include chronic diarrhea, mesenteric lymphadenopathy and anorexia. • Dysfunction of any organ system may result from granuloma formation within the tissue of that organ, e.g., liver, kidney, spleen, intestines, lungs, etc., however, organ failure producing clinical signs only rarely occurs, and most dysfunction is only detected on biochemical tests. Clinical signs in the acute, fatal form of extraintestinal disease are caused primarily by tissue damage from the rapidly dividing tachyzoites. • Young kittens are more likely to have gastrointestinal signs, although mild clinical disease has been reported in adult cats as well. Systemic signs, which are not present in all cats, include fever, anorexia, lethargy, vomiting, diarrhea and lymphadenopathy. Systemic signs such as fever, anorexia and depression are commonly reported (44% of cats) and can be seen with skin lesions.


id: cord-022243-lahg6xlm
title: The cat with a head tilt, vestibular ataxia or nystagmus
author: Parent, Joane M
date: 2009-05-15
txt: ./txt/cord-022243-lahg6xlm.txt
cache: ./cache/cord-022243-lahg6xlm.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7155481/
doi: 10.1016/b978-0-7020-2488-7.50043-0
abstract: nan
summary:
  • By close proximity, the neurological structures associated with the middle ear may be affected leading to facial nerve paresis/paralysis, dry eye from decreased to absent lacrimation, and/or Acute to peracute non-progressive onset of a head tilt with ipsilateral falling or rolling in an otherwise healthy cat. Diagnosis is based on careful history taking (to disclose if there is somnolence or quietness of the animal), physical, neurological, otoscopic and ophthalmoscopic (including Schirmer tear test) examinations, serum protein concentration, cerebrospinal fluid analysis (CSF), CSF anti-coronavirus IgG titer, electrodiagnostic testing (brain auditoryevoked responses), bullae radiography, computed tomography (CT) and magnetic resonance imaging (MRI) scan. The history of an older cat presented with a rapid onset of neurological signs relating to the inner (vestibular signs and deafness) and middle ear (facial paralysis, decreased lacrimation and Horner''s syndrome) with pain upon jaw opening and a swollen face increases the index of suspicion.


id: cord-022283-8ny6j1ny
title: The weak and ataxic or paralyzed cat
author: Cuddon, Paul A
date: 2009-05-15
txt: ./txt/cord-022283-8ny6j1ny.txt
cache: ./cache/cord-022283-8ny6j1ny.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7155525/
doi: 10.1016/b978-0-7020-2488-7.50047-8
abstract: nan
summary:
  Most cats with spinal cord disease have a combination of both ataxia and paresis, since most myelopathies cause disruption of both the motor and sensory systems. Cats presenting solely with ataxia and paresis/paralysis most commonly have spinal cord disease. The most common causes of spinal cord ataxia and paresis in cats are infectious (including feline infectious peritonitis virus (coronavirus)), neoplasia (lymphosarcoma) and trauma. Infectious diseases, such as feline infectious peritonitis, toxoplasmosis and cryptococcosis also may produce signs of progressive spinal cord dysfunction. Many cats with sacrococcygeal trauma also show signs of LMN paraparesis (sciatic nerve injury), consisting of dragging of the hind paws on their dorsum and a failure to flex the pelvic limb(s) when walking or when the withdrawal reflex is performed. Cats with severe myelopathy or cauda equina injury with analgesia have a very poor to hopeless prognosis since they commonly have physical or functional spinal cord or cauda equina transection. Feline polioencephalomyelitis is a chronic, progressive disease affecting the spinal cord and brain of cats.


id: cord-022520-ebj51v9o
title: Biology and Diseases of Ferrets
author: Marini, Robert P.
date: 2007-09-02
txt: ./txt/cord-022520-ebj51v9o.txt
cache: ./cache/cord-022520-ebj51v9o.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7158191/
doi: 10.1016/b978-012263951-7/50016-8
abstract: nan
summary:
  Campylobacter jejuni is a gram-negative, spirally curved microaerophilic bacterium that is recognized as a significant cause of human enteritis and is as-sociated with diarrheic illness in several animal species, including dogs, cats, cows, goats, pigs, mink, ferrets, and sheep (Carter et al., 1995) . Reports of spontaneous cases in ferrets require diagnostic confirmation and differentiation from cases of proliferative bowel disease and other infectious and noninfectious causes of diarrhea. Systemic infection with the bovine strain in ferrets results in disseminated disease with weight loss, anorexia, lethargy, death, and miliary lesions involving the lungs and other viscera (Fox, 1998a) . Clinical disease may occur in kits as young as 1-4 days old or in older animals up to 6 weeks of age. Other potential etiologies that have been considered include two infectious agents that are known to cause chronic immune stimulation in affected ferrets, the Aleutian disease virus (ADV) and Helicobacter mustelae.


id: cord-022526-j9kg00qf
title: Disorders of the Gastrointestinal System
author: Jones, Samuel L.
date: 2009-05-18
txt: ./txt/cord-022526-j9kg00qf.txt
cache: ./cache/cord-022526-j9kg00qf.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7158198/
doi: 10.1016/b0-72-169777-1/50015-9
abstract: nan
summary:
  Examination of the cardiovascular system (heart, peripheral pulse, and mucous membranes), lungs, and abdomen is essential to detect clinical signs of systemic inflammation from endotoxemia, coagulation disorders, dehydration, ileus, shock, and other abnormalities resulting from injury to the small or large intestine. Several reports suggest the efficacy of cisapride in managing intestinal disease in horses, including the resolution of persistent large colon impaction, treatment of equine grass sickness, and as a preventative for POI in horses after small intestinal surgery (0.1 mg/kg body mass intramuscularly during the postoperative period). 9 Primary role-players in DPJ-associated ileus include peritoneal inflammation, inflammatory cell migration/activation within the muscularis, small intestinal mechanical distention, and effects of endotoxin absorption. Diarrhea probably results from the severe ulceration and inflammation of the large intestine, causing increased secretion of water, electrolytes, and protein and decreased absorption of fluid.


id: cord-022555-a7ie82fs
title: Digestive System, Liver, and Abdominal Cavity
author: nan
date: 2011-12-05
txt: ./txt/cord-022555-a7ie82fs.txt
cache: ./cache/cord-022555-a7ie82fs.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7158306/
doi: 10.1016/b978-1-4377-0660-4.00023-5
abstract: nan
summary:
  One study found that, of cats investigated for gastrointestinal disease, 9 of 33 cats (27%) had no pathology recognized proximal to the jejunum (i.e., the effective length of diagnostic endoscopes would have precluded diagnosis), and other organs were affected in 9 of 10 cats with inflammatory bowel diseases and 7 of 8 cats with intestinal small cell lymphoma. 60, 64 Quantification of serum cobalamin levels is recommended in cats with clinical signs of small bowel diarrhea, ones suspected to have an infiltrative disease of the small intestine (inflammatory bowel disease or gastrointestinal lymphoma), or ones with pancreatic dysfunction. Survey radiographs may be normal in cats with esophagitis and strictures, but are useful to rule out other causes for the clinical signs, such as a foreign body, or to detect related problems, such as aspiration pneumonia. 8, 29 Other non-neoplastic causes reported for gastric or gastroduodenal ulceration in cats include parasites (e.g., Ollulanus tricuspis, Toxocara cati, Aonchotheca putorii, Gnathostoma spp.), bacterial infections, toxins, inflammatory bowel disease, and foreign bodies.


id: cord-022575-ybj6lwdb
title: Vestibular Disorders
author: Platt, Simon R.
date: 2009-05-15
txt: ./txt/cord-022575-ybj6lwdb.txt
cache: ./cache/cord-022575-ybj6lwdb.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7158340/
doi: 10.1016/b0-72-160423-4/50059-7
abstract: nan
summary:
  1, 3 Signs of central vestibular syndrome suggest brainstem involvement and are not present in patients with inner ear disease except in cases of direct extension of the disease process, 8 such as can be seen with otitis media/interna 9 and neoplasia. Horner''s syndrome (miosis, ptosis, enophthalmos, and protrusion of the third eyelid) of the ipsilateral eye may be present with middle or inner ear disease, causing peripheral vestibular dysfunction ( Figure 56 -11). Peripheral vestibular dysfunction results from disease of the middle and inner ear affecting the receptors in the labyrinth and the vestibular portion of cranial nerve VIII. Seven such cats with otitis media/interna have been documented, in one study, with CNS dysfunction that included central vestibular signs. Peripheral vestibular disease in a cat with middle and inner ear squamous cell carcinoma Tympanic bulla osteotomy for treatment of middle-ear disease in cats: 19 cases (1984-1991)


id: cord-023165-f6o6owg3
title: Diseases of the Gastrointestinal System
author: NAVARRE, CHRISTINE B.
date: 2009-05-21
txt: ./txt/cord-023165-f6o6owg3.txt
cache: ./cache/cord-023165-f6o6owg3.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7167521/
doi: 10.1016/b0-72-169052-1/50006-5
abstract: nan
summary:
  The most important reason for examining feces in sheep and goats is to determine the presence and relative number of nematode parasites infesting an animal or flock. Clinical signs of frothy bloat and free gas bloat from either food intake or physical obstruction of the esophagus are usually more severe and immediately life-threatening than bloat seen from rumen wall diseases and systemic influences. Rumen acidosis usually occurs in animals that have been fed predominantly forage-based rations and are suddenly given access to large amounts of highly fermentable concentrates or concentrated forms of energy. Table 4 -2 lists the agents most likely to cause diarrhea in lambs and kids, tissues or other samples required for diagnosis, and commonly employed test methods. Liver abscesses usually occur as a result of chronic rumenitis in cattle, but they are rare in sheep and goats. F. hepatica infestation usually causes acute disease in sheep and goats but can present as a chronic condition.


id: cord-023367-ujflw19b
author: Newcomer, Benjamin W.
date: 2020-04-17
txt: ./txt/cord-023367-ujflw19b.txt
cache: ./cache/cord-023367-ujflw19b.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7169350/
doi: 10.1016/b978-0-323-62463-3.00025-6
abstract: nan
summary:
  The cause of transformation is usually unknown; in rare cases, especially in flock outbreaks in sheep, it can be linked to exposure to the bovine leukemia virus, which has occurred experimentally and as a result of the administration of whole blood Anaplasma vaccines. C. perfringens type C in older sheep causes the disease known as "struck." Affected animals usually are found dead or with signs of toxemia. The course of the disease is usually very short (0.5-12 hours), so sudden or spontaneous death is a common clinical sign across affected small ruminant species. Additional evidence of systemic toxemia (metabolic acidosis, azotemia, and increases in liver and muscle enzymes) also may be seen; however, diagnosis of black disease is based on characteristic history (endemic liver fluke areas), clinical signs, and postmortem findings and testing.

title:
  Diseases of the hematologic, immunologic, and lymphatic systems (multisystem diseases) [Image: see text]


id: cord-026009-rdhuc2n2
title: Pet Rodents
author: Anderson, Nancy L.
date: 2009-05-15
txt: ./txt/cord-026009-rdhuc2n2.txt
cache: ./cache/cord-026009-rdhuc2n2.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7271187/
doi: 10.1016/b0-72-160422-6/50179-0
abstract: nan
summary:
  This chapter provides information needed to diagnose and treat the most frequently encountered problems of mice, rats, gerbils, hamsters, guinea pigs, and chinchillas. • Diagnosis is based on clinical signs, history, visualization of parasite, skin scrape, and cellophane tape test. • Clinical signs in adults are caused by secondary bacterial infections and are similar to those in MRM. Common primary or secondary pathogens causing respiratory signs in mice are Streptococcus pneumoniae, Corynebacterium kutscheri, Pasteurella pneumontropica, Pseudomonas aeruginosa, and Klebsiella pneumoniae. • Mouse poliomyelitis/encephalomyelitis, also known as Theiler disease, causes clinical signs in 1 in 10,000 infected mice. • In contrast to mice, Sendai virus rarely causes clinical signs in rats. • Pneumonia in guinea pigs usually is caused by infection with S. • Diagnosis of scurvy is based on clinical signs, the exclusion of other causes of diarrhea, and response to vitamin C therapy (see Table 177 -10).


id: cord-026031-hnf5vayd
title: Emergency Care
author: Ford, Richard B.
date: 2009-05-21
txt: ./txt/cord-026031-hnf5vayd.txt
cache: ./cache/cord-026031-hnf5vayd.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7271342/
doi: 10.1016/b0-72-160138-3/50002-3
abstract: nan
summary:
  Fresh whole blood Coagulopathy with active hemorrhage (disseminated intravascular coagulation, thrombocytopenia; massive acute hemorrhage; no stored blood available) Stored whole blood Massive acute or ongoing hemorrhage; hypovolemic shock caused by hemorrhage that is unresponsive to conventional crystalloid and colloid fluid therapy; unavailability of equipment required to prepare blood components Packed red blood cells Nonregenerative anemia, immune-mediated hemolytic anemia, correction of anemia before surgery, acute or chronic blood loss Fresh frozen plasma Factor depletion associated with active hemorrhage (congenital: von Willebrand''s factor, hemophilia A, hemophilia B; acquired: vitamin K antagonist, rodenticide intoxication, DIC); acute or chronic hypoproteinemia (burns, wound exudates, body cavity effusion; hepatic, renal, or gastrointestinal loss); colostrum replacement in neonates Frozen plasma Acute plasma or protein loss; chronic hypoproteinemia; (contains stable colostrum replacement in neonates; hemophilia B and clotting factors) selected clotting factor deficiencies Platelet-rich plasma* Thrombocytopenia with active hemorrhage (immune-mediated thrombocytopenia, DIC); platelet function abnormality (congenital: thrombasthenia in Bassett hounds; acquired: NSAIDs, other drugs) Cryoprecipitate


id: cord-253125-93r1aokh
author: Barreiro, Luis B.
date: 2006-04-05
txt: ./txt/cord-253125-93r1aokh.txt
cache: ./cache/cord-253125-93r1aokh.txt
extension: .txt
mime: text/plain
url: https://www.sciencedirect.com/science/article/pii/S0198885906000164
doi: 10.1016/j.humimm.2006.02.028
summary:
  title: DC-SIGN Interacts with Mycobacterium leprae but Sequence Variation in This Lectin Is Not Associated with Leprosy in the Pakistani Population Here we sought to evaluate whether DC-SIGN interacts with the leprosy bacillus, Mycobacterium leprae, and whether DC-SIGN genetic variation influences the susceptibility and/or pathogenesis of the disease. Our most recent results show that nucleotide variation in the DC-SIGN promoter region is associated to susceptibility to tuberculosis [7] . leprae, we performed cold binding assays using fluorescently labeled bacilli and DC-SIGN-expressing recombinant HeLa cells as previously described [5, 11] . In this light, to investigate whether variation in the coding and/or the cis-regulatory regions of DC-SIGN is involved in susceptibility to and clinical outcome of leprosy, we conducted an association (case/control) study based on a sequencing/genotyping strategy in a cohort of patients presenting the two polarities of the disease and a group of healthy controls.

title:
  DC-SIGN Interacts with Mycobacterium leprae but Sequence Variation in This Lectin Is Not Associated with Leprosy in the Pakistani Population

abstract:
  The C-type lectin DC-SIGN is involved in early interactions between human innate immune cells and a variety of pathogens. Here we sought to evaluate whether DC-SIGN interacts with the leprosy bacillus, Mycobacterium leprae, and whether DC-SIGN genetic variation influences the susceptibility and/or pathogenesis of the disease. A case–control study conducted in a cohort of 272 individuals revealed no association between DC-SIGN variation and leprosy. However, our results clearly show that DC-SIGN recognizes M. leprae, indicating that mycobacteria recognition by this lectin is not as narrowly restricted to the Mycobacterium tuberculosis complex as previously thought. Altogether, our results provide further elucidation of M. leprae interactions with the host innate immune cells and emphasize the importance of DC-SIGN in the early interactions between the human host and the infectious agents.


id: cord-265600-lnik974k
title: Role of DC-SIGN and L-SIGN receptors in HIV-1 vertical transmission
author: Celerino da Silva, Ronaldo
date: 2011-01-26
txt: ./txt/cord-265600-lnik974k.txt
cache: ./cache/cord-265600-lnik974k.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pubmed/21277928/
doi: 10.1016/j.humimm.2011.01.012
summary:
  Some PRRs located on the surface of dendritic cells (DCs) and other cells seem to play an important role in human immunodeficiency virus type 1 (HIV-1) transmission. Dendritic cell–specific intercellular adhesion molecule–3 grabbing non-integrin, CD209 (DC-SIGN) and its homolog, DC-SIGN-related (DC-SIGNR or L-SIGN) receptors are PPRs able to bind the HIV-1 gp120 envelope protein and, because alterations in their expression patterns also occur, they might play a role in both horizontal and vertical transmission as well as in disseminating the virus within the host. This review aims to explore the involvement of the dendritic cell-specific intercellular adhesion molecule-3 grabbing non-integrin, CD209 (DC-SIGN) and DC-SIGN-related C-type lectin domain family 4, member M (L-SIGN) receptors in HIV-1 transmission from mother to child. Transmission of the HIV-1 virus from mother to child via breast milk can occur by free virus particles and/or viral particles associated with cells [4] ; in this case, the expression of cellular receptors for recognition and adhesion of pathogens is required.

abstract:
  The innate immune system acts in the first line of host defense against pathogens. One of the mechanisms used involves the early recognition and uptake of microbes by host professional phagocytes, through pattern recognition receptors (PRRs). These PRRs bind to conserved microbial ligands expressed by pathogens and initiate both innate and adaptative immune responses. Some PRRs located on the surface of dendritic cells (DCs) and other cells seem to play an important role in human immunodeficiency virus type 1 (HIV-1) transmission. Dendritic cell–specific intercellular adhesion molecule–3 grabbing non-integrin, CD209 (DC-SIGN) and its homolog, DC-SIGN-related (DC-SIGNR or L-SIGN) receptors are PPRs able to bind the HIV-1 gp120 envelope protein and, because alterations in their expression patterns also occur, they might play a role in both horizontal and vertical transmission as well as in disseminating the virus within the host. This review aims to explore the involvement of the DC-SIGN and L-SIGN receptors in HIV-1 transmission from mother to child.


id: cord-266226-gxbrgy6g
author: Lee, Choongho
date: 2019-10-06
txt: ./txt/cord-266226-gxbrgy6g.txt
cache: ./cache/cord-266226-gxbrgy6g.txt
extension: .txt
mime: text/plain
url: https://doi.org/10.3390/md17100567
doi: 10.3390/md17100567
summary:
  In particular, a red algae-derived griffithsin (GRFT) protein has demonstrated superior in vitro and in vivo antiviral activity with minimum host toxicity against a variety of clinically relevant, enveloped viruses. mGRFT possesses greatly reduced antiviral activity against HIV-1 in spite of its comparable association with high-mannose oligosaccharides, since mGRFT possesses all three carbohydrate-binding sites [20] . Combinations of GRFT and other carbohydrate-binding agents (CBAs) including Hippeastrum hybrid agglutinin, Galanthus nivalis agglutinin, a mannose-specific monoclonal antibody (mAb) (2G12), microvirin, and banana lectin also showed synergistic activity against HIV-1, HIV-2, and even against certain CBA-resistant HIV-1 strains [28] . In this regard, GRFT''s ability to partially block gp120 from binding to human DC-SIGN [34] and its potent inhibition of DC-SIGN-dependent transfer of HIV-1 [38] could synergize with its antiviral action by blocking viral entry. Monomerization of viral entry inhibitor griffithsin elucidates the relationship between multivalent binding to carbohydrates and anti-HIV activity

title:
  Griffithsin, a Highly Potent Broad-Spectrum Antiviral Lectin from Red Algae: From Discovery to Clinical Application

abstract:
  Virus entry into a susceptible host cell is the first step in the formation of all viral diseases. Controlling viral infections by disrupting viral entry is advantageous for antibody-mediated neutralization by the host’s immune system and as a preventive and therapeutic antiviral strategy. Recently, several plant-derived carbohydrate-binding proteins (lectins) have emerged as a new class of antiviral biologics by taking advantage of a unique glycosylation pattern only found on the surface of viruses. In particular, a red algae-derived griffithsin (GRFT) protein has demonstrated superior in vitro and in vivo antiviral activity with minimum host toxicity against a variety of clinically relevant, enveloped viruses. This review examines the structural characteristics of GRFT, focusing on its carbohydrate-binding capability. Its in vitro antiviral profiles against human immunodeficiency virus (HIV) are also discussed followed by a description of the results from a combination study using anti-HIV drugs. The results of several studies regarding its novel antiviral mechanism of action are provided in conjunction with an explanation of viral resistance profiles to GRFT. In addition, its in vitro and in vivo host toxicity profiles are summarized with its pharmacokinetic behavior using in vivo efficacy study results. Also, a large-scale production and formulation strategy, as well as a drug delivery strategy, for GRFT as a new class of broad-spectrum microbicides is discussed. Finally, results from two ongoing clinical studies examining GRFT’s effects on viruses are presented.


id: cord-267234-waz0k0ms
author: Shu, Chang
date: 2015-01-13
txt: ./txt/cord-267234-waz0k0ms.txt
cache: ./cache/cord-267234-waz0k0ms.txt
extension: .txt
mime: text/plain
url: https://api.elsevier.com/content/article/pii/S0145305X15000051
doi: 10.1016/j.dci.2015.01.004
summary:
  Dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN/CD209) and liver/lymph node-specific ICAM-grabbing non-integrin (L-SIGN/CD299) which are homologues of DC-SIGN are important members in C-type lectin receptors family as key molecules to recognize and eliminate pathogens in the innate immune system. The sequence analysis results showed that mmDC-SIGN and mmL-SIGN have the same domains with other vertebrates except primates, and share some conserved motifs in CRD among all the vertebrates which play a crucial role in interacting with Ca(2+) and for recognizing mannose-containing motifs. In this study, we analyzed genomic organizations, gene structures, and synteny, evolutionary process and expression of miiuy croaker DC-SIGN (mmDC-SIGN) and L-SIGN (mmL-SIGN). Among these fish genomes, genes from TTC8 to ENTPD5 located downstream of L-SIGN had conserved synteny only differing in no RABEPK gene in miiuy croaker and no RABEPK and ALDH6A1 in stickleback. Another phylogenetic tree of L-SIGN genes constructed by Bayesian approach (Fig. 2C ) was used to test the positive selection in ancestral lineages of fishes.

title:
  Characterization of the duplicate L-SIGN and DC-SIGN genes in miiuy croaker and evolutionary analysis of L-SIGN in fishes

abstract:
  Dendritic cell-specific ICAM-3-grabbing non-integrin (DC-SIGN/CD209) and liver/lymph node-specific ICAM-grabbing non-integrin (L-SIGN/CD299) which are homologues of DC-SIGN are important members in C-type lectin receptors family as key molecules to recognize and eliminate pathogens in the innate immune system. DC-SIGN and L-SIGN have become hot topics in recent studies which both served as cell adhesion and phagocytic pathogen recognition receptors in mammals. However, there have been almost no studies of DC-SIGN and L-SIGN structure and characters in fish, only DC-SIGN in the zebrafish had been studied. In our study, we identified and characterized the full-length miiuy croaker (Miichthys miiuy) DC-SIGN (mmDC-SIGN) and L-SIGN (mmL-SIGN) genes. The sequence analysis results showed that mmDC-SIGN and mmL-SIGN have the same domains with other vertebrates except primates, and share some conserved motifs in CRD among all the vertebrates which play a crucial role in interacting with Ca(2+) and for recognizing mannose-containing motifs. Gene synteny of DC-SIGN and L-SIGN were analyzed for the first time and gene synteny of L-SIGN was conserved among the five fishes. Interestingly, one gene next to L-SIGN from gene synteny had high similarity with L-SIGN gene that was described as L-SIGN-like in fish species. While only one L-SIGN gene existed in other vertebrates, two L-SIGN in fish may be in consequence of the fish-specific genome duplication to adapt the specific environment. The evolutionary analysis showed that the ancestral lineages of L-SIGN gene in fishes experienced purifying selection and the current lineages of L-SIGN gene in fishes underwent positive selection, indicating that the ancestral lineages and current lineages of L-SIGN gene in fishes underwent different evolutionary patterns. Both mmDC-SIGN and mmL-SIGN were expressed in all tested tissues and ubiquitously up-regulated in infected liver, spleen and kidney at different sampling time points, indicating that the mmDC-SIGN and mmL-SIGN participated in the immune response to defense against bacteria infection.


id: cord-267269-05mezubh
author: Plazolles, N.
date: 2010-10-12
txt: ./txt/cord-267269-05mezubh.txt
cache: ./cache/cord-267269-05mezubh.txt
extension: .txt
mime: text/plain
url: https://doi.org/10.1189/jlb.0710386
doi: 10.1189/jlb.0710386
summary:
  Previous studies have reported that TM-lacking encoding DC-SIGN sequences are transcribed as soluble cytoplasmic pro-teins but not secreted by the sDC-SIGN-expressing transfectant cells or immature MoDCs [19] . Thus, using our quantitative and specific ELISA, we observed the presence of potential sDC-SIGN isoforms in 10ϫ concentrated cell culture supernatants of mDC-SIGN-expressing DCs. In vitro DCs were generated from adult monocytes or CD34 ϩ CBPs, according to already well-known protocols [17, 23, 30] . Despite the use of high concentrations of Marimastat (10 M), no modification of sDC-SIGN versus mDC-SIGN expression patterns could be observed, thus weighing in favor of a sliced, sequence-derived product and not a shedding of mDC-SIGN by MMPs. Like many cell types, DCs are able to secrete 60 -80 nm membrane vesicles, called exosomes. In addition, as mDC-SIGN expression was reported to be responsible for MoDC CMV cis-infection, we assumed that FLAG-sDC-SIGN1AT1 may function as a promoter of the infection.

title:
  Pivotal Advance: The promotion of soluble DC‐SIGN release by inflammatory signals and its enhancement of cytomegalovirus‐mediated cis‐infection of myeloid dendritic cells

abstract:
  DC‐SIGN is a member of the C‐type lectin family. Mainly expressed by myeloid DCs, it is involved in the capture and internalization of pathogens, including human CMV. Several transcripts have been identified, some of which code for putative soluble proteins. However, little is known about the regulation and the functional properties of such putative sDC‐SIGN variants. To better understand how sDC‐SIGN could be involved in CMV infection, we set out to characterize biochemical and functional properties of rDC‐SIGN as well as naturally occurring sDC‐SIGN. We first developed a specific, quantitative ELISA and then used it to detect the presence sDC‐SIGN in in vitro‐generated DC culture supernatants as cell‐free secreted tetramers. Next, in correlation with their inflammatory status, we demonstrated the presence of sDC‐SIGN in several human body fluids, including serum, joint fluids, and BALs. CMV infection of human tissues was also shown to promote sDC‐SIGN release. Based on the analysis of the cytokine/chemokine content of sDC‐SIGN culture supernatants, we identified IFN‐γ and CXCL8/IL‐8 as inducers of sDC‐SIGN production by MoDC. Finally, we demonstrated that sDC‐SIGN was able to interact with CMV gB under native conditions, leading to a significant increase in MoDC CMV infection. Overall, our results confirm that sDC‐SIGN, like its well‐known, counterpart mDC‐SIGN, may play a pivotal role in CMV‐mediated pathogenesis.


id: cord-267671-ys43n672
title: Biology and Diseases of Mice
author: Whary, Mark T.
date: 2015-07-10
txt: ./txt/cord-267671-ys43n672.txt
cache: ./cache/cord-267671-ys43n672.txt
extension: .txt
mime: text/plain
url: https://api.elsevier.com/content/article/pii/B9780124095274000031
doi: 10.1016/b978-0-12-409527-4.00003-1
summary:
  Clinical Signs MCMV causes subclinical infection in adult immunocompetent mice, but experimental inoculation of neonates can cause lethal disease due to multisystemic necrosis and inflammation. Diagnosis Because infected mice do not manifest signs or lesions and the virus is very difficult to propagate in cell culture, detection and diagnosis rely on serology and molecular methods. Differential Diagnosis Reovirus infection must be differentiated from other diarrheal diseases of infant mice, including those caused by mouse coronaviruses, EDIM virus, Salmonella spp., or Clostridium piliforme. Epizootiology EDIM virus appears to be infectious only for mice and occurs episodically in mouse colonies, and infection is probably widespread geographically (Livingston and Riley, 2003; Pritchett-Corning LABORATORY ANIMAL MEDICINE et al., 2009) . Sentinel mouse surveillance, using soiled bedding, is an effective strategy for detecting MNV (Manuel et al., 2008) Differential Diagnosis The mild change in fecal consistency associated with MNV in adult mice may mimic rotavirus, coronavirus, Helicobacter spp., Citrobacter rodentium, or other enteric diseases.

abstract:
  Today’s laboratory mouse, Mus musculus, has its origins as the ‘house mouse’ of North America and Europe. Beginning with mice bred by mouse fanciers, laboratory stocks (outbred) derived from M. musculus musculus from eastern Europe and M. m. domesticus from western Europe were developed into inbred strains. Since the mid-1980s, additional strains have been developed from Asian mice (M. m. castaneus from Thailand and M. m. molossinus from Japan) and from M. spretus which originated from the western Mediterranean region.


id: cord-268902-npug5c8p
title: The Roles of Direct Recognition by Animal Lectins in Antiviral Immunity and Viral Pathogenesis
author: Liu, Yang
date: 2015-01-29
txt: ./txt/cord-268902-npug5c8p.txt
cache: ./cache/cord-268902-npug5c8p.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pubmed/25642837/
doi: 10.3390/molecules20022272
summary:
  In agreement with the findings in mosquitoes, a recent study has identified a C-type lectin in the shrimp Marsupenaeus japonicus that interacts with an envelope protein of White spot syndrome virus (WSSV) and consequently associates with a cell-surface calreticulin, which serves as a membrane receptor that facilitates viral entry in a cholesterol-dependent manner [128] . The interaction between lectins and viral glycoproteins may lead to the three following consequences: (1) lectins, such as MBL and SPs, function as pattern recognition molecules that bind a repertoire of viruses and activate antiviral immune responses; (2) lectins are employed as attachment factors that recruit viral particles to the cell membrane to enhance viral entry, e.g., some mammalian lectins (DC-SIGN, L-SIGN, MR and MPRs) or their homologs in arthropods (mosGCTLs); and (3) some intracellular lectins, such as calnexin and ERGIC-53, function as susceptibility factors associated with virus-encoded proteins to facilitate viral replication or assembly (please refer to Figures 1 and 4) .

abstract:
  Lectins are a group of proteins with carbohydrate recognition activity. Lectins are categorized into many families based on their different cellular locations as well as their specificities for a variety of carbohydrate structures due to the features of their carbohydrate recognition domain (CRD) modules. Many studies have indicated that the direct recognition of particular oligosaccharides on viral components by lectins is important for interactions between hosts and viruses. Herein, we aim to globally review the roles of this recognition by animal lectins in antiviral immune responses and viral pathogenesis. The different classes of mammalian lectins can either recognize carbohydrates to activate host immunity for viral elimination or can exploit those carbohydrates as susceptibility factors to facilitate viral entry, replication or assembly. Additionally, some arthropod C-type lectins were recently identified as key susceptibility factors that directly interact with multiple viruses and then facilitate infection. Summarization of the pleiotropic roles of direct viral recognition by animal lectins will benefit our understanding of host-virus interactions and could provide insight into the role of lectins in antiviral drug and vaccine development.


id: cord-271505-eot38721
title: Molecular pathogenesis of severe acute respiratory syndrome
author: Wang, Hongliang
date: 2006-09-28
url: https://www.ncbi.nlm.nih.gov/pubmed/17142081/
doi: 10.1016/j.micinf.2006.06.012
abstract:
  The global outbreak in 2002–2003 of severe acute respiratory syndrome (SARS) posed a serious threat to public health and had a significant impact on socioeconomic stability. Although the global outbreak of SARS has been contained, there are serious concerns over its re-emergence and bioterrorism potential, and up to date, no specific treatment exists for this disease. Here we review the progress of studies on the pathogenesis of the disease, in particular, studies on the molecular level.


id: cord-275863-qos9vu3r
title: Lectin Switching During Dengue Virus Infection
author: Dejnirattisai, Wanwisa
date: 2011-06-15
txt: ./txt/cord-275863-qos9vu3r.txt
cache: ./cache/cord-275863-qos9vu3r.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pubmed/21606536/
doi: 10.1093/infdis/jir173
summary:
  In this report we have studied the interaction of dengue viruses produced in insect cells, tumor cell lines, and primary human dendritic cells (DCs) with DC-SIGN and L-SIGN. To formally prove that the loss of infection of DCs was a result of the loss of affinity of DC-produced virus for DC-SIGN, we went on to test infection on 3T3 cells expressing DC-SIGN and included in these assays the related C-type lectin L-SIGN ( Figure 3A ), which has also been reported to be a receptor for dengue virus. C6/36-and DC-derived viruses were incubated with increasing levels of pooled convalescent dengue immune serum and subsequently used to infect U937, a monocyte cell line that expresses the Fc receptor and which shows relatively low infectivity without the presence of enhancing antibodies. Viruses produced in both DCs and insect cells were susceptible to enhancement, over the same range of antibody concentrations, showing that DC-produced virus could exploit ADE to replicate in individuals undergoing a secondary dengue infection ( Figure 6A ).

abstract:
  Dengue virus receptors are relatively poorly characterized, but there has been recent interest in 2 C-type lectin molecules, dendritic cell–specific intercellular adhesion molecule 3 (ICAM-3)–grabbing nonintegrin (DC-SIGN) and its close homologue liver/lymph node–specific ICAM-3–grabbing integrin (L-SIGN), which can both bind dengue and promote infection. In this report we have studied the interaction of dengue viruses produced in insect cells, tumor cell lines, and primary human dendritic cells (DCs) with DC-SIGN and L-SIGN. Virus produced in primary DCs is unable to interact with DC-SIGN but remains infectious for L-SIGN–expressing cells. Skin-resident DCs may thus be a site of initial infection by insect-produced virus, but DCs will likely not participate in large-scale virus replication during dengue infection. These results reveal that differential glycosylation of dengue virus envelope protein is highly dependent on cell state and suggest that studies of virus tropism using virus prepared in insect cells or tumor cell lines should be interpreted with caution.


id: cord-279343-ybncwweg
author: Snyder, Greg A.
date: 2005-04-15
txt: ./txt/cord-279343-ybncwweg.txt
cache: ./cache/cord-279343-ybncwweg.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pubmed/15784257/
doi: 10.1016/j.jmb.2005.01.063
summary:
  The dendritic cell-specific ICAM-3 non-integrin (DC-SIGN) and its close relative DC-SIGNR recognize various glycoproteins, both pathogenic and cellular, through the receptor lectin domain-mediated carbohydrate recognition. On the basis of the current crystal structure and other published structures with sequence homology to the repeat domain, we generated a tetramer model for DC-SIGN/R using homology modeling and propose a ligand-recognition index to identify potential receptor ligands. [23] [24] [25] Modeling of the DC-SIGN/R tetramer A homology search was performed using sequences corresponding to various lengths of the repeat domain of DC-SIGNR against known structures in the Protein Data Bank (PDB). 21 On the basis of the current crystal structures and available biophysical data, a tetramer for the entire extracellular DC-SIGNR receptor was constructed by homology modeling in which the repeat regions form helical bundles to bring together their CRDs in a 4-fold related symmetry.

title:
  The Structure of DC-SIGNR with a Portion of its Repeat Domain Lends Insights to Modeling of the Receptor Tetramer

abstract:
  The dendritic cell-specific ICAM-3 non-integrin (DC-SIGN) and its close relative DC-SIGNR recognize various glycoproteins, both pathogenic and cellular, through the receptor lectin domain-mediated carbohydrate recognition. While the carbohydrate-recognition domains (CRD) exist as monomers and bind individual carbohydrates with low affinity and are permissive in nature, the full-length receptors form tetramers through their repeat domain and recognize specific ligands with high affinity. To understand the tetramer-based ligand binding avidity, we determined the crystal structure of DC-SIGNR with its last repeat region. Compared to the carbohydrate-bound CRD structure, the structure revealed conformational changes in the calcium and carbohydrate coordination loops of CRD, an additional disulfide bond between the N and the C termini of the CRD, and a helical conformation for the last repeat. On the basis of the current crystal structure and other published structures with sequence homology to the repeat domain, we generated a tetramer model for DC-SIGN/R using homology modeling and propose a ligand-recognition index to identify potential receptor ligands.


id: cord-287799-ridm3qd7
title: S-layer proteins of Lactobacillus acidophilus inhibits JUNV infection
author: Martínez, María Guadalupe
date: 2012-06-15
txt: ./txt/cord-287799-ridm3qd7.txt
cache: ./cache/cord-287799-ridm3qd7.txt
extension: .txt
mime: text/plain
url: https://doi.org/10.1016/j.bbrc.2012.05.031
doi: 10.1016/j.bbrc.2012.05.031
summary:
  Among those, Junin virus (JUNV) entry is enhanced in cells expressing DC-SIGN and for that reason surface-layer protein (S-layer) of Lactobacillus acidophilus ATCC 4365 was evaluated as a possible JUNV inhibitor. Experiments using 3T3 cells stably expressing DC-SIGN, showed an almost complete inhibition of JUNV infection when they were treated with S-layer in a similar extend as the inhibition shown by mannan. Since 3T3 cells are poorly infect by JUNV in the absence of expression of C-type lectins this model provides a really strong tool to study the effect of S-layer protein on the infection enhanced by DC-SIGN or L-SIGN. We presumed that the C-terminal portion of the S-layer would be responsible of the interaction with the glycan strand of DC-SIGN, since we have already shown it to interact with cell wall peptidoglycan [3] and it has been reported, that two repeats sequences in the C-terminal portion of the protein showed homology to carbohydrate binding domains (CBD) of Clostridium difficile S-layer/ toxin [27, 28] .

abstract:
  It has been previously described that S-layer binds to the C-type lectin DC-specific ICAM-3-grabbing nonintegrin (DC-SIGN, CD209). It was also shown that DC-SIGN is a cell-surface adhesion factor that enhances viral entry of several virus families. Among those, Junin virus (JUNV) entry is enhanced in cells expressing DC-SIGN and for that reason surface-layer protein (S-layer) of Lactobacillus acidophilus ATCC 4365 was evaluated as a possible JUNV inhibitor. Experiments using 3T3 cells stably expressing DC-SIGN, showed an almost complete inhibition of JUNV infection when they were treated with S-layer in a similar extend as the inhibition shown by mannan. However no inhibition effect was observed in 3T3 wild type cells or in 3T3 cells expressing liver/lymph node-specific ICAM-3 grabbing nonintegrin (L-SIGN or DC-SIGNR or CD209L). Treatments with S-layer during different times in the infection demonstrated that inhibition was only observed when S-layer was presented in early stages of the viral infection. This inhibition does not involve the classic recognition of mannose by this C-type lectin as the S-layer showed no evidence to be glycosylated. In fact, the highly basic nature of the S-layer (pI > 9.5) seems to be involved in electrostatic interactions between DC-SIGN and S-layer, since high pH abolished the inhibitory effect on infection cause by the S-layer. In silico analysis predicts a Ca(2+)-dependant carbohydrate recognition domain in the SlpA protein. This novel characteristic of the S-layer, a GRAS status protein, contribute to the pathogen exclusion reported for this probiotic strain and may be applied as an antiviral agent to inhibit several kinds of viruses.


id: cord-293151-g3758oes
title: Biology and Diseases of Dogs
author: Nemzek, Jean A.
date: 2015-07-10
txt: ./txt/cord-293151-g3758oes.txt
cache: ./cache/cord-293151-g3758oes.txt
extension: .txt
mime: text/plain
url: https://api.elsevier.com/content/article/pii/B9780124095274000122
doi: 10.1016/b978-0-12-409527-4.00012-2
summary:
  This provides the necessary background to discuss the spontaneous diseases, including infectious and neoplastic conditions, prevalent in purpose bred as well as random source dogs used in biomedical research. Several factors that increase pressure at the site and/or affect the integrity of the skin will predispose an individual to develop pressure sores, including poor hygiene, self-trauma, low-protein diet, preexisting tissue damage, muscle wasting, inadequate bedding, and ill-fitting coaptation devices (Swaim and Angarano, 1990) . Chronic or recurrent corneal ulcers may also be associated with infection or hereditary causes in some breeds of dogs; however, these would be rare in the laboratory setting. Research Complications Treatment of early-stage or low-grade mammary tumors may be rewarding, allowing dogs to continue on study.

abstract:
  Historically, the dog played an important role as a laboratory animal in biomedical research. Although numbers are declining, the use of dogs continues to be common in pharmacokinetics and cardiovascular studies. The normal biology of the dog as both a laboratory and a companion animal has been well studied and reference values are presented here as a clinical and experimental resource. This provides the necessary background to discuss the spontaneous diseases, including infectious and neoplastic conditions, prevalent in purpose bred as well as random source dogs used in biomedical research. In addition, diseases and conditions that arise secondary to the housing and experimental manipulation of dogs is discussed with emphasis on treatment and prevention.


id: cord-300272-95o8yd7h
author: Thépaut, Michel
date: 2020-08-10
txt: ./txt/cord-300272-95o8yd7h.txt
cache: ./cache/cord-300272-95o8yd7h.txt
extension: .txt
mime: text/plain
url: https://doi.org/10.1101/2020.08.09.242917
doi: 10.1101/2020.08.09.242917
summary:
  In the context of the current COVID-19 pandemic, attention is now focused on the SARS-CoV-2 virus Zhou et al., 2020) .Coronaviruses use a homotrimeric glycosylated spike (S) protein protruding from their viral envelope to interact with cell membranes and promote fusion upon proteolytic activation. Additionally, in the case of SARS-CoV-2, a new paradigm is needed to untangle the complex clinical picture, resulting in a vast range of possible symptoms and in a spectrum of disease severity associated on one hand with active viral replication and cell infection through interaction with ACE2 along the respiratory tract, and, on the other hand, to the development of excessive immune activation, i.e. the so called "cytokine storm", that is related to additional tissue damage and potential fatal outcomes. These observations prompted us to investigate the potential interaction of C-type lectins receptors, notably DC/L-SIGN with SARS-CoV-2, through glycan recognition of the spike envelope glycoprotein, as well at their potential role in SARS-CoV-2 transmission.

title:
  DC/L-SIGN recognition of spike glycoprotein promotes SARS-CoV-2 trans-infection and can be inhibited by a glycomimetic antagonist

abstract:
  The efficient spread of SARS-CoV-2 resulted in a pandemic that is unique in modern history. Despite early identification of ACE2 as the receptor for viral spike protein, much remains to be understood about the molecular events behind viral dissemination. We evaluated the contribution of C-type lectin receptors (CLRS) of antigen-presenting cells, widely present in air mucosa and lung tissue. DC-SIGN, L-SIGN, Langerin and MGL bind to diverse glycans of the spike using multiple interaction areas. Using pseudovirus and cells derived from monocytes or T-lymphocytes, we demonstrate that while virus capture by the CLRs examined does not allow direct cell infection, DC/L-SIGN, among these receptors, promote virus transfer to permissive ACE2+ cells. A glycomimetic compound designed against DC-SIGN, enable inhibition of this process. Thus, we described a mechanism potentiating viral capture and spreading of infection. Early involvement of APCs opens new avenues for understanding and treating the imbalanced innate immune response observed in COVID-19 pathogenesis


id: cord-304720-0lgup7yj
title: Swine Diseases and Disorders
author: Robbins, R.C.
date: 2014-08-21
txt: ./txt/cord-304720-0lgup7yj.txt
cache: ./cache/cord-304720-0lgup7yj.txt
extension: .txt
mime: text/plain
url: https://api.elsevier.com/content/article/pii/B9780444525123001340
doi: 10.1016/b978-0-444-52512-3.00134-0
summary:
  The industry significance, etiology, epidemiology, pathogenesis, clinical signs, postmortem and histpathologic lesions, diagnostic testing, and generic treatment, control, and prevention are described. Important history to understand from caretakers includes: age of pigs affected, duration of clinical signs, morbidity rate, mortality rate, treatments administered, response to treatments, and any other important information regarding previous diagnoses or disease in the affected group of animals. Records include but are not limited to: where the animals originated from; number in the herd; age; daily mortality; number treated; name of treatment, route of delivery and dose; feed and water usage; high-low temperatures; and vaccinations received or administered. Postweaning infections result in a high morbidity but low mortality; most significant economic losses at this time are caused by reduced average daily gain, market weights, and overall system efficiency. Postweaning infections result in a high morbidity but low mortality; most significant economic losses at this time are caused by reduced average daily gain, market weights, and overall system efficiency.

abstract:
  Swine diseases and disorders that are significant in modern, commercial swine production systems are organized by body system; the reader will need to know basic anatomy and physiology. The industry significance, etiology, epidemiology, pathogenesis, clinical signs, postmortem and histpathologic lesions, diagnostic testing, and generic treatment, control, and prevention are described. Diseases of a particular system are summarized in a differential diagnosis table.


id: cord-308412-m4u1ax8k
title: Analysis of 4 imaging features in patients with COVID-19
author: Jin, Jun
date: 2020-07-23
txt: ./txt/cord-308412-m4u1ax8k.txt
cache: ./cache/cord-308412-m4u1ax8k.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pubmed/32703209/
doi: 10.1186/s12880-020-00484-1
summary:
  The following CT image features were observed for each patient: (a) the location, extent, and a number of lesions; (b) type of lesions (GGO, vascular thickening, pulmonary consolidation, pulmonary fibrous, interlobular septum, and solid nodules); (c) specific signs ("air bronchogram sign", "feather sign", "dandelion sign", "pomegranate sign", "rime sign"); (d) other signs (pleural effusion, mediastinal lymphadenectasis,etc). c A partially enlarged image at the same level as in figure b, suggesting that the GGO in the posterior basal segment of the left lower lobe showed a "pomegranate sign" (red arrow) Fig. 4 A older male patient who experienced constipation, and anorexia lasting for 1 week, and who had no epidemiological history. In the present study, we found that the most common CT imaging features in patients with COVID-19 were: bilateral, multifocal GGO, peripheral distribution; the predominant lower lobe; pleural effusion and lymphadenectasis were rare, which is consistent with previous reports [6] [7] [8] .

abstract:
  BACKGROUND: The aim of this was to analyze 4 chest CT imaging features of patients with coronavirus disease 2019 (COVID-19) in Shenzhen, China so as to improve the diagnosis of COVID-19. METHODS: Chest CT of 34 patients with COVID-19 confirmed by the nucleic acid test (NAT) were retrospectively analyzed. Analyses were performed to investigate the pathological basis of four imaging features(“feather sign”,“dandelion sign”,“pomegranate sign”, and “rime sign”) and to summarize the follow-up results. RESULTS: There were 22 patients (65.2%) with typical “feather sign”and 18 (52.9%) with “dandelion sign”, while few patients had “pomegranate sign” and “rime sign”. The “feather sign” and “dandelion sign” were composed of stripe or round ground-glass opacity (GGO), thickened blood vessels, and small-thickened interlobular septa. The “pomegranate sign” was characterized as follows: the increased range of GGO, the significant thickening of the interlobular septum, complicated with a small amount of punctate alveolar hemorrhage. The “rime sign” was characterized by numerous alveolar edemas. Microscopically, the wall thickening, small vascular proliferation, luminal stenosis, and occlusion, accompanied by interstitial infiltration of inflammatory cells, as well as numerous pulmonary interstitial fibrosis and partial hyaline degeneration were observed. Repeated chest CT revealed the mediastinal lymphadenectasis in one patient. Re-examination of the NAT showed another positive anal swab in two patients. CONCLUSION: “Feather sign” and “dandelion sign” were typical chest CT features in patients withCOVID-19; “pomegranate sign” was an atypical feature, and “rime sign” was a severe feature. In clinical work, accurate identification of various chest CT signs can help to improve the diagnostic accuracy of COVID-19 and reduce the misdiagnosis or missed diagnosis rate.


id: cord-322617-znvikfza
title: Role of the C-type lectins DC-SIGN and L-SIGN in Leishmania interaction with host phagocytes
author: Caparrós, Esther
date: 2005-08-19
url: https://www.ncbi.nlm.nih.gov/pubmed/16164025/
doi: 10.1016/j.imbio.2005.05.013
abstract:
  Leishmaniasis is a parasitic disease that courses with cutaneous or visceral clinical manifestations. The amastigote stage of the parasite infects phagocytes and modulates the effector function of the host cells. Our group has described that the interaction between Leishmania and immature monocyte-derived dendritic cells (DCs) takes place through dendritic cell-specific ICAM-3-grabbing nonintegrin (DC-SIGN), a C-type lectin that specifically recognizes fungal, viral and bacterial pathogens. The DC-SIGN-mediated recognition of Leishmania amastigotes does not induce DC maturation, and the DC-SIGN ligand/s on Leishmania parasites is/are still unknown. We have also found that the DC-SIGN-related molecule L-SIGN, specifically expressed in lymph node and liver sinusoidal endothelial cells, acts as a receptor for L. infantum, the parasite responsible for visceral leishmaniasis, but does not recognize L. pifanoi, which causes the cutaneous form of the disease. Therefore, DC-SIGN and L-SIGN differ in their ability to interact with Leishmania species responsible for either visceral or cutaneous leishmaniasis. A deeper knowledge of the parasite-C-type lectin interaction may be helpful for the design of new DC-based therapeutic vaccines against Leishmania infections.


id: cord-333655-lylt7qld
title: Bitter‐sweet symphony: glycan–lectin interactions in virus biology
author: Van Breedam, Wander
date: 2013-12-06
txt: ./txt/cord-333655-lylt7qld.txt
cache: ./cache/cord-333655-lylt7qld.txt
extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pubmed/24188132/
doi: 10.1111/1574-6976.12052
summary:
  In sum, it appears that the dimeric lectin galectin-1 can enhance HIV-1 infection efficiency by cross-linking viral and host cell glycans and thereby promoting firmer adhesion of the virus to the target cell surface and facilitating virus-receptor interactions (Ouellet et al., 2005; Mercier et al., 2008; St-Pierre et al., 2011; Sato et al., 2012) . As has been shown for IAV, acquisition or deletion of glycosylation sites may affect crucial steps in the viral infection/replication process (e.g. receptor binding, fusion, release of newly formed virions) (Ohuchi et al., 1997; Wagner et al., 2000; Tsuchiya et al., 2002; Kim & Park, 2012) , alter the capacity of the virus to avoid induction of/recognition by virus-specific antibodies (glycan shielding) Wei et al., 2010; Wanzeck et al., 2011; Kim & Park, 2012; Job et al., 2013; Sun et al., 2013) , and modulate viral interaction with various immune system lectins (Reading et al., 2007; Vigerust et al., 2007; Reading et al., 2009; Tate et al., 2011a, b) .

abstract:
  Glycans are carbohydrate modifications typically found on proteins or lipids, and can act as ligands for glycan‐binding proteins called lectins. Glycans and lectins play crucial roles in the function of cells and organs, and in the immune system of animals and humans. Viral pathogens use glycans and lectins that are encoded by their own or the host genome for their replication and spread. Recent advances in glycobiological research indicate that glycans and lectins mediate key interactions at the virus‐host interface, controlling viral spread and/or activation of the immune system. This review reflects on glycan–lectin interactions in the context of viral infection and antiviral immunity. A short introduction illustrates the nature of glycans and lectins, and conveys the basic principles of their interactions. Subsequently, examples are discussed highlighting specific glycan–lectin interactions and how they affect the progress of viral infections, either benefiting the host or the virus. Moreover, glycan and lectin variability and their potential biological consequences are discussed. Finally, the review outlines how recent advances in the glycan–lectin field might be transformed into promising new approaches to antiviral therapy.


id: cord-342936-43u7afl3
title: Targeting the glycans of glycoproteins: a novel paradigm for antiviral therapy
author: Balzarini, Jan
date: 2007
txt: ./txt/cord-342936-43u7afl3.txt
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mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pubmed/17632570/
doi: 10.1038/nrmicro1707
summary:
  Perhaps more importantly, such carbohydrate-binding agents (CBAs) may force the virus to delete at least part of its glycan shield to escape drug pressure 5 ; this might result in the initiation of an immune response against uncovered immunogenic envelope epitopes. Although such a mechanism may be efficient for a first-line inactivation of HIV, CBA-exposed HIV strains may decrease the efficiency of LCs to eliminate HIV, but at the same time may compromise the ability of the virus to be efficiently transmitted by DCs. The interactions of several CBAs have been extensively investigated, including: the prokaryotic CV-N and actinohivin; a variety of plant lectins, including Hippeastrum hybrid agglutinin (HHA) and UDA; the non-peptidic low-molecular-weight antibiotic PRM-A; and the monoclonal antibody 2G12 with the HIV-envelope gp120 and/or several glycan structures.

abstract:
  Several chronic viral infections (such as HIV and hepatitis C virus) are highly prevalent and are a serious health risk. The adaptation of animal viruses to the human host, as recently exemplified by influenza viruses and the severe acute respiratory syndrome coronavirus, is also a continuous threat. There is a high demand, therefore, for new antiviral lead compounds and novel therapeutic concepts. In this Review, an original therapeutic concept for suppressing enveloped viruses is presented that is based on a specific interaction of carbohydrate-binding agents (CBAs) with the glycans present on viral-envelope glycoproteins. This approach may also be extended to other pathogens, including parasites, bacteria and fungi.


id: cord-344124-1ztyj0z4
title: Virus entry: old viruses, new receptors
author: Backovic, Marija
date: 2012-01-02
txt: ./txt/cord-344124-1ztyj0z4.txt
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extension: .txt
mime: text/plain
url: https://www.ncbi.nlm.nih.gov/pubmed/22440960/
doi: 10.1016/j.coviro.2011.12.005
summary:
  The long-sought entry receptors for rubella, sindbis and respiratory syncytial viruses (RV, SV and RSV), together with the missing measles virus (MV) receptor for infection of epithelial cells, were identified in 2011. The long-sought entry receptors for rubella, sindbis and respiratory syncytial viruses (RV, SV and RSV), together with the missing measles virus (MV) receptor for infection of epithelial cells, were identified in 2011. In addition, 2011 was rich in new information about the interactions of MV, RSV and phleboviruses with DC-SIGN during infection of dendritic cells, a crucial step allowing the virus to breach the epithelial barrier and gain access to the lymph nodes. For instance, for the arbovirus SV, which was also shown to interact with DCs via DC-SIGN for reaching the lymph nodes [47] , the studies discussed below have now identified an entry receptor -NRAMP -that is more likely to be used in these further stages of the infection, and perhaps at all stages, since it is very well conserved between humans and mosquitoes.

abstract:
  The long-sought entry receptors for rubella, sindbis and respiratory syncytial viruses (RV, SV and RSV), together with the missing measles virus (MV) receptor for infection of epithelial cells, were identified in 2011. These have been major developments in the field of virus entry. In addition, 2011 was rich in new information about the interactions of MV, RSV and phleboviruses with DC-SIGN during infection of dendritic cells, a crucial step allowing the virus to breach the epithelial barrier and gain access to the lymph nodes. This faciliates dissemination to susceptible tissues where it can develop a vigorous and sustained replication, to eventually target specific organs from which it can propagate into the environment and efficiently infect new hosts, closing the merry-go-round of the virus cycle.


