cord-000079-533xlisc	2009	Both, lymphocytic choriomeningitis virus glycoprotein (LCMV-GP) and vesicular stomatitis virus glycoprotein (VSV-G) pseudotyped lentiviral vectors very efficiently transduced human glioblastoma cells in vitro and in vivo. In a therapeutic approach using the suicide gene herpes simplex virus thymidine kinase (HSV-1-tk) fused to eGFP, both lentiviral vectors mediated a complete remission of solid tumors as seen on MRI resulting in a highly significant survival benefit (p<0.001) compared to control groups. Furthermore, we showed a significant therapeutic effect of LCMV-GP pseudotyped lentiviral vectors in the cell-line based 9L rat glioma model using the suicide gene HSV-1-tk. In the presented work, we showed that both, VSV-G and LCMV-GP pseudotyped lentiviruses efficiently transduced human glioma cells in vitro and in vivo, whereas gammaretroviral transduction was inefficient. When analyzed at higher magnification, both LCMV-GP and VSV-G pseudotyped lentiviral vectors showed efficient transgene delivery to nestin-positive tumor cells in solid ( Figure 3B ,E) and invasive tumor areas ( Figure 3C ,F).
cord-000660-tsvzg0ax	2012	Interferon protects mice from vesicular stomatitis virus (VSV) infection and pathogenesis; however, it is not known which of the numerous interferon-stimulated genes (ISG) mediate the antiviral effect. In contrast, in acute infection by viruses that cause severe pathogenesis and death within a few days after infection, protection is primarily provided by the intrinsic antiviral actions of IFN-induced proteins encoded by the hundreds of IFN-stimulated genes (ISGs) [10] [11] [12] , several of which often contribute to the overall effect of IFN against a given virus. From the above observations, we conclude that after intranasal infection by VSV, Ifit2 protects mice from neuropathogenesis by suppressing replication or spread of the virus in brain neurons. In the complete absence of type I IFN action in the IFNAR 2/2 mice, intranasally infected VSV replicated vigorously not only in brains, but also in livers and lungs ( Figure 7A-C) .
cord-001765-7wv4cb37	2015	One of these rVSV vectors (N4CT1-EBOVGP1), which expresses membrane-anchored EBOV GP from the first position in the genome (GP1), elicited a balanced cellular and humoral GP-specific immune response in mice. Guinea pigs immunized with a single dose of this vector were protected from any signs of disease following lethal EBOV challenge, while control animals died in 7-9 days. Guinea pigs immunized with a single dose of this vector were protected from any signs of disease following lethal EBOV challenge, while control animals died in 7-9 days. The studies described here are the first to demonstrate protection of guinea pigs and macaques with a single dose of highly attenuated rVSV expressing EBOVGP, and we believe that the N4CT1-EBOVGP1 vector has the essential safety and efficacy characteristics for use in a vaccine to prevent EBOV infection in humans and the great apes.
cord-003667-u1xa44nw	2019	Based on the results of these initial pilot studies, we elected to adjust vaccine and challenge doses, and administered 10 7 pfu/dose of the replication competent virus (ΔGrVSV-CCHFV-GPCΔ) to prime and boosted groups of five STAT-1 −/− mice, respectively (Fig. 3) . Regardless, protection was achieved by both regimens, although the boosted group data suggests that at study endpoint, the observed IgG titers against CCHFV-GPC along with lower neutralizing titers (PRNT 50 of < 1:320) are evidence of the ability to combat lethal CCHFV infection in the STAT-1 −/− mouse model after vaccination (Fig. 5A,B) . Now that we have established that this new vector can provide protective benefit, our future studies will temporally examine the antibody and T cell repertoire after prime and boosting doses following ΔGrVSV-CCHFV-GPCΔ, but before CCHFV challenge, as these would be informative for the STAT-1 −/− mouse model.
cord-004126-u6ts87ur	2020	Moreover, single vaccination induced cross-protective H5-specific antibodies and protected mice against lethal challenge with various H5 clade 2 viruses, highlighting the potential of the VSV-based HAfl as a pan-H5 influenza virus emergency vaccine. We found that a single vaccination with VSV-vectors expressing the full-length HA (HAfl) induced crossreactive H5-specific antibodies and conferred complete protection against lethal challenge with various H5 clade 2 viruses. In contrast to all the sHA-based vaccines, single doses of the VSV-EBOV-HAfl or VSV-HAfl vectors were sufficient to provide complete protection from lethal homologous H5N1 challenge in mice (Fig. 2) . However, this study did not provide any data supporting an advantage of including VSV-EBOV as part of the vector design over just expressing VSV-HAfl as both vectors performed similarly well with no statistically significant difference in efficacy following single-dose or prime/boost administration (Fig. 2 ) nor in antibody responses (Fig. 3, Table 1 ).
cord-004733-i0a3igc7	1992	title: Identification of epitopes associated with different biological activities on the glycoprotein of vesicular stomatitis virus by use of monoclonal antibodies Thirteen monoclonal antibodies (MAbs) to the glycoprotein (G) of vesicular stomatitis virus (VSV) serotype Indiana were prepared and examined for their effects on various biological activities of VSV, including in vitro infection, hemagglutination, adsorption to cells, and mediation of cell fusion. Many enveloped viruses including vesicular stomatitis virus (VSV), family Rhabdoviridae, genus Vesiculovirus, transfer their nucleocapsids to the cytoplasm of host cells by the adsorption and receptor-mediated endocytosis, followed by fusion with the endosomal membrane [20, 21] . In the present study, we prepared thirteen MAbs specific for seven distinct epitopes on G protein of VSV-Indiana and examined for their effects on various biological activities of VSV including in vitro infection, HA, adsorption to the cells, and mediation of cell-cell fusion.
cord-008556-oetrdm8g	2008	One consequence of the scanning mechanism is that deleting the "ribosome binding site" (i.e., the normal initiator codon and flanking sequences) will not abolish translation; ribosomes will simply use the next AUG codon downstream, which, in some cases, has been shown to direct the synthesis of a biologically active, truncated protein (Downey et al., 1984; Halpern and Smiley, 1984; Katinka and Yaniv, 1982) . The best evidence for this is the ability of both EMC and SFV 26 S mRNA to be translated in EMC virus-infected cells, in which host translation is drastically inhibited by a mechanism that has not been difined, but that clearly does not involve cap binding protein (Mosenkis et al., 1985) . In wild-type adenovirus-infected cells, in which host protein synthesis is drastically reduced, both adenovirus and influenza virus mRNAs are translated efficiently.
cord-011435-x73foqu7	2020	title: High Throughput Screening of FDA-Approved Drug Library Reveals the Compounds that Promote IRF3-Mediated Pro-Apoptotic Pathway Inhibit Virus Replication Previously, we uncovered a function for nontranscriptional IRF3 (nt-IRF3), RLR (RIG-I-like receptor)-induced IRF3-mediated pathway of apoptosis (RIPA), which triggers apoptotic killing of virus-infected cells. In contrast to the transcriptional pathway, nt-Irf3 in virus-infected cells functions as a chaperone protein by translocating the pro-apoptotic protein BCL2-associated X (BAX) to the mitochondria, thereby causing apoptotic cell death, which we named RLR (RIG-I-like receptor)-induced IRF3-mediated pathway of apoptosis (RIPA) ( Figure 1A ) [7] [8] [9] [10] [11] [12] [13] . We validated these results by immunoblot analyses, which demonstrate that doxorubicin treatment inhibited the expression of VSV-G protein, a viral envelope glycoprotein as well as the virus-encoded GFP ( Figure 3B ). We validated these results by immunoblot analyses, which demonstrate that doxorubicin treatment inhibited the expression of VSV-G protein, a viral envelope glycoprotein as well as the virus-encoded GFP ( Figure 3B ).
cord-020714-h1fevqcw	2008	
cord-104239-xxlcdbqi	1996	
cord-262752-bwofzbwa	2017	Early work by Witte and colleagues showed that when they used VSV to infect the cells in which MLV is packaged, they were able to harvest pseudovirus for use in neutralization antibody assays. Development of in vitro and in vivo rabies virus neutralization assays based on a high-titer pseudovirus system Development of a pseudotyped-lentiviral-vector-based neutralization assay for chikungunya virus infection Second generation of pseudotype-based serum neutralization assay for Nipah virus antibodies: sensitive and high-throughput analysis utilizing secreted alkaline phosphatase Use of vesicular stomatitis virus pseudotypes bearing Hantaan or Seoul virus envelope proteins in a rapid and safe neutralization test A neutralization test for specific detection of Nipah virus antibodies using pseudotyped vesicular stomatitis virus expressing green fluorescent protein Truncation of the human immunodeficiency virus-type-2 envelope glycoprotein allows efficient pseudotyping of murine leukemia virus retroviral vector particles Cholesterol supplementation during production increases the infectivity of retroviral and Lentiviral vectors pseudotyped with the vesicular stomatitis virus glycoprotein (VSV-G)
cord-262753-jld1ygxt	2019	
cord-267712-mhx8e5y0	2012	Due to its potent capabilities in triggering cellular, humoral, and mucosal immunities in animals, even after a single administration, recombinant VSV has been studied as a vaccine vector not only for preventing vesicular stomatitis disease in livestock [4] , but a number of human pathogens including: Influenza virus, Ebola virus, Marburg virus, Human immunodeficiency (HIV) virus, Severe Acute Respiratory Syndrome (SARS) virus, and Hepatitis C virus [5] [6] [7] [8] [9] . In vivo, however, VSV M protein mutant proved to be only moderately attenuated in experimental infections [16, 21] , whereas there is currently no information available if recombinant VSV with truncated G protein is safe or not when animals challenged with high dose of the mutant virus. Based on pathogenicity and capabilities to stimulate potent immune responses, we aimed to identify a suitable recombinant VSV vaccine vector and vaccine candidate for preventing vesicular stomatitis disease.
cord-268565-2sg1tlrg	2006	However, because durable neutralizing antibodies are usually elicited against the VSV surface glycoprotein after a single vaccination with replication-competent rVSV vectors, glycoprotein exchange vectors were designed to allow more effective boosting of immune responses to target antigens. In these pioneering studies, rhesus macaques were immunized with a combination of two prototypic rVSV vectors expressing a HIV-1 89.6 Env gp160/VSV-G fusion polypeptide and simian immunodeficiency virus (SIV) Gag p55 protein. Vaccine vector administration by a combination of intramuscular and intranasal routes clearly demonstrated the ability of rVSV vectors to elicit potent antigen-specific cellmediated immune responses in NHPs. In addition, this study also clearly demonstrated for the first time the ability of rVSV vectors expressing Env and Gag proteins to provide highly significant protection from AIDS after an intravenous heterologous SIV/HIV (SHIV) 89 .6P challenge [89] . Immunogenicity of attenuated vesicular stomatitis virus vectors expressing HIV type 1 Env and SIV Gag proteins: comparison of intranasal and intramuscular vaccination routes
cord-270380-1me7ugkg	2020	Both proteins exhibited effective anti-vesicular stomatitis virus (VSV) activity in Vero, F81 (feline kidney cell), Madin–Darby bovine kidney (MDBK), Madin–Darby canine kidney (MDCK), and porcine kidney (PK-15) cells, showing broader cross-species antiviral activity than the INTERCAT IFN antiviral drug. Furthermore, the recombinant feIFN-ωa and feIFN-ωb proteins demonstrated antiviral activity against VSV, feline coronavirus (FCoV), canine parvovirus (CPV), bovine viral diarrhea virus (BVDV), and porcine epidemic diarrhea virus (PEDV), indicating better broad-spectrum antiviral activity than the INTERCAT IFN. As shown in Figure 6 , the purified recombinant feIFN-ωa and feIFN-ωb proteins showed antiviral activity in both homologous animal cells (F81 cells) and heterologous animal cells (Vero, MDCK, MDBK, and PK-15 cells) in vitro. Our data showed that purified recombinant feIFN-ωa and feIFN-ωb had broad-spectrum antiviral activity in homologous and heterologous animal cells, suggesting they are candidates for the development of effective therapeutic agents to be used against viral infections in pet cats.
cord-272051-arz8r204	2011	Since the replication of many virus species requires the activity of host cell proteases, investigating the effects of PIs on the life cycle of viruses other than HIV would be of interest. Considering that PIs are well tolerated drugs in vivo, and that many relevant human pathogens belong to the family of RNA viruses infecting cells through an endocytic pathway, this finding would open the way towards a broader therapeutic use of PIs. HIV virions emerging from cells treated with PIs remain immature viral particles as a consequence of the block of Gag polyprotein cleavage. Cells were treated overnight with the PI doses most effective against VSV and/or influenza virus replication, then labeled with LysoSensor Green DND-189 for 30 min in the presence of PIs, and finally analyzed by FACS.
cord-275348-jna496x7	2008	A SARS vaccine based on a live-attenuated vesicular stomatitis virus (VSV) recombinant expressing the SARS-CoV S protein provides long-term protection of immunized mice from SARS-CoV infection (Kapadia, S.U., Rose, J. We found that the vaccine given intramuscularly induced a neutralizing antibody response to SARS-CoV that was approximately ten-fold greater than that required for the protection from SARS-CoV infection, and significantly greater than that generated by the replication-competent vector expressing SARS-CoV S protein given by the same route. In order to evaluate this vector as a SARS vaccine candidate, we also developed a SARS-CoV neutralization assay using a pseudotyped VSV recombinant expressing a green fluorescent protein. SARS-CoV neutralizing antibody titers of these sera were determined by incubating VSVΔG-EGFP/SΔtail-HA virus with serial dilutions of these sera, and the virusserum mixtures were transferred to a monolayer of Vero E6 cells.
cord-276009-p98wjtjb	2009	
cord-277823-vijh6x1l	2019	A serological survey of Middle East respiratory syndrome coronavirus (MERS-CoV) was conducted among dromedary camels and herbivorous animals sharing the same pasturage in Ethiopia. One of camel serum that showed a high antibody titer in the neutralization test by live MERS-CoV was treated as a positive control. According to the results of the previous study, antibody titers of ≥16 are treated as positive in neutralization test using VSV-MERS/GFP. Cows that were antibody positive in the neutralization test using VSV-MERS/GFP or cELISA were different animals and both were antibody negative in the neutralization test using MERS-CoV. S1-ELISA was not sensitive compared to other tests because only 16 serum samples were positive and they required an antibody titer of ≥64 in VSV-MERS/GFP. The present study shows that the neutralization test using VSV-MERS/GFP, S1-ELISA, and cELISA are as specific to MERS-CoV infection as the serological tests, although their sensitivities slightly differ. Middle East respiratory syndrome coronavirus neutralising serum antibodies in dromedary camels: a comparative serological study
cord-285749-0ejhd9nw	2016	Generation of VSV pseudotypes (VSVpp) was performed as follows: HEK-293T cells were transfected by calcium-phosphate precipitation with expression plasmids encoding viral surface proteins, VSV-G (positive control) , NiV-F/G, FLUAV-HA and/or NA and bat-FLUAV-HAL and/or NAL, or empty plasmid (pCAGGS) as negative control. In order to investigate the potential of human TTSPs to proteolytically activate batFLUAV-HAL for host cell entry, we additionally cotransfected the cells with expression plasmids for TMPRSS2, DESC-1 or MSPL. Notably, three bat cell lines (EidNi/41, HypNi/1.1 and EpoNi/22.1) were susceptible to entry of pseudotypes bearing HAL and NAL of batFLUAV (Fig 2B) , demonstrating that surface glycoproteins of batFLUAV can mediate cellular entry. To assess proteolytic activation of HA/HAL proteins, vesicular stomatitis virus-based pseudotypes (VSVpp) were produced in cells transfected to express the indicated type II transmembrane serine proteases (B) or different amounts of TMPRSS2 (C).
cord-286390-ytgw3j4s	2020	An anticipated correlate of such countermeasures is the level of neutralizing antibodies against the SARS-CoV-2 spike protein, which engages with host ACE2 receptor for entry. Using an infectious molecular clone of vesicular stomatitis virus (VSV) expressing eGFP as a marker of infection, we replaced the glycoprotein gene (G) with the spike protein of SARS-CoV-2 (VSV-eGFP-SARS-CoV-2) and developed a high-throughput imaging-based neutralization assay at biosafety level 2. We engineered an infectious molecular clone of vesicular 83 stomatitis virus (VSV) to encode the SARS-CoV-2 S protein in place of the native envelope 84 glycoprotein (G) and rescued an autonomously replication-competent virus bearing the spike. Evaluation of a novel vesicular stomatitis virus pseudotype-based assay for detection of 641 neutralizing antibody responses to SARS-CoV Vesicular stomatitis virus pseudotyped with severe acute 645 respiratory syndrome coronavirus spike protein Retroviruses pseudotyped with the severe acute respiratory 722 syndrome coronavirus spike protein efficiently infect cells expressing angiotensin-converting 723 enzyme 2
cord-290243-m8yfugr0	2007	The resulting residue was purified by silica gel column chromatography using hexane and ethyl acetate (5:1) as the eluent to give the corresponding alcohol 8 (5.570 g, 95%) as a colorless oil: ½a To a stirred solution of alcohol 8 (3.050 g, 6.19 mmol) in anhydrous CH 2 Cl 2 (20 mL) was dropwise added (dieth-ylamino)sulfur trifluoride (DAST, 1.23 mL, 9.31 mmol) at À10°C and the reaction mixture was stirred at the same temperature for 30 min. After the volatiles were removed in vacuo, the resulting residue was purified by silica gel column chromatography using hexane and ethyl acetate (3:1) as the eluent to give To a stirred solution of 13 (110 mg, 0.19 mmol) in methanol (4.5 mL) and CH 2 Cl 2 (1.5 mL) was added 1 M NaOMe (0.40 mL, 0.40 mmol, in MeOH) at 0°C and the reaction mixture was stirred for 6 h at room temperature.
cord-291323-kbjyd5g3	2020	We describe here potent inhibitory effects on content release and infection by chimeric vesicular stomatitis virus (VSV) containing the envelope proteins of Zaire ebolavirus (VSV-ZEBOV) or severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) (VSV-SARS-CoV-2) elicited by Apilimod and Vacuolin-1, small-molecule inhibitors of the main endosomal phosphatidylinositol-3-phosphate/phosphatidylinositol 5-kinase, PIKfyve. We describe here potent inhibitory effects on content release and infection by chimeric vesicular stomatitis virus (VSV) containing the envelope proteins of Zaire ebolavirus (VSV-ZEBOV) or severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) (VSV-SARS-CoV-2) elicited by Apilimod and Vacuolin-1, small-molecule inhibitors of the main endosomal phosphatidylinositol-3-phosphate/phosphatidylinositol 5-kinase, PIKfyve. We have constructed chimeric forms of vesicular stomatitis virus (VSV) bearing the fusion proteins of Zaire ebolavirus (ZEBOV) or SARS coronavirus 2 (SARS-CoV-2) and shown that two small-molecule inhibitors of an endosomal lipid kinase (PIKfyve) inhibit viral infection by preventing release of the viral contents from endosomes.
cord-292593-apdyaujt	1985	Interference with vesicular stomatitis virus (VSV) production by JHMV was tested in persistently or latently infected RN-2 cells using as the controls, uninfected RN2-2 cells. Since upon infection of RN2-2 cultures with JHMV at 39.5"C and maintenance in a state of latency at that temperature for several days, the cells commenced yielding pfu upon shift down to 32.5"C (Lucas et al., 1978) , these data suggest that penetration and eclipse of the virus inoculum must have occurred normally at 39.5"C and restriction most probably developed at a subsequent stage. It is very significant that during incubation at the restrictive temperature for as long as 7 days and beyond, when RN2-2 cells had multiplied through 6-7 generations, the 56K antigen was readily detectable (channel I), implying that during latency, in the absence of infectious virus production, translation into JHMV nucleocapsid protein continued.
cord-296187-nnv2e7gr	2020	The SARS-CoV-2 spike glycoprotein, due to its primary interaction with the human angiotensin-converting enzyme 2 (ACE2) cell-surface receptor, is considered as a potential target for drug development. Based on in silico screening followed by in vitro studies, here we report that the existing FDA-approved Bcr-Abl tyrosine kinase inhibitor, imatinib, inhibits SARS-CoV-2 with an IC50 of 130 nM. We provide evidence that although imatinib binds to the receptor-binding domain (RBD) of SARS-CoV-2 spike protein with an affinity at micromolar, i.e., 2.32 ± 0.9 μM levels, imatinib does not directly inhibit the spike RBD:ACE2 interaction – suggesting a Bcr-Abl kinase-mediated fusion inhibition mechanism is responsible for the inhibitory action. This study utilizes in silico methodology followed by in vitro experimental validation to screen existing FDA-approved small molecule drugs specific to the RBD of the spike protein of SARS-CoV-2 to identify repurposable drugs targeting further clinical validation.
cord-296399-vvbjulm9	2017	
cord-296466-hakaoo9i	2006	
cord-299281-5z1xminb	1993	
cord-316589-f1hq0xl5	2020	Our results indicate that high intrahepatic doses of VSV-FH did not result in any significant toxicity and were well tolerated by transgenic mice expressing the measles virus receptor CD46. Furthermore, single intratumoral treatments with VSV-FH yielded improved survival and complete tumor regressions in a proportion of mice in the Hep3B hepatocellular carcinoma model, but not in mice xenografted with BxPC3 pancreatic cancer cells. In this study, we evaluated whether treatment with oncolytic VSV-FH could trigger a potent cytotoxicity effect in HBPC cell lines in vitro and in vivo using animal models. Safety studies on intrahepatic or intratumoral injection of oncolytic vesicular stomatitis virus expressing interferon-beta in rodents and nonhuman primates High CD46 receptor density determines preferential killing of tumor cells by oncolytic measles virus Vesicular stomatitis virus expressing interferon-beta is oncolytic and promotes antitumor immune responses in a syngeneic murine model of non-small cell lung cancer
cord-318587-ewvnkdr2	2020	
cord-318686-we6pveus	2016	CONCLUSION: In the current study, we showed that newly established cell lines from the cotton rat can serve as host-specific in vitro models for viral infection experiments. The cotton rat (Sigmodon hispidus) is a unique example of a rodent species that is a well-established animal model to study viral pathogenesis and is also associated with a large range of zoonotic viruses in the wild [20] [21] [22] . To evaluate whether the broad viral susceptibility seen in both animalmodel and wild cotton rats was also reflected in in vitro cell culture models, we generated continuous cell lines from the respiratory and renal tracts of a cotton rat, and assessed their use for virus replication studies of known and potentially novel zoonotic viruses. In the work presented herein, we generated epithelial cell lines from the respiratory and renal tracts of a cotton rat due to its susceptibility to a broad range of human viruses, as well as the association of multiple important and emerging zoonotic viruses with this species.
cord-324674-yd7idp90	2018	ADP/P2Y 13 -mediated protection against viral infection operates by suppressing the expression of exchange protein activated by cAMP 1 (EPAC1), which is an alternative key intracellular sensor for cAMP. To our surprise, the RNA replication of VSV in ADP-treated RAW264.7 cells was reduced significantly in a time-( Figure 2D ) and concentration-( Figure 2E ) dependent manner. To explore the key receptors involved in ADP-mediated antiviral activities, we detected the expression of P2Y 1 , P2Y 12 , and P2Y 13 after VSV infection. ADP/P2Y 13 restricts viral replication by inhibiting cAMP signaling Type I IFN plays pivotal roles in fighting against the invaded virus, so we tested whether it was involved in ADP/P2Y 13mediated antiviral activities. As shown in Figure 7A , when infected RAW264.7 cells with VSV, NDV, and HSV-1, RNA expression of EPAC1 was increased significantly.
cord-326013-5i35zdmv	2020	The data justify clinical studies investigating whether amitriptyline, a safe drug used clinically for almost 60 years, or other antidepressants that functionally block acid sphingomyelinase prevent SARS-CoV-2 infection. Pretreatment of the cells with 5, 10, 20, or 25 µM amitriptyline prevented the activation of acid sphingomyelinase and the release of ceramide upon infection with pp-VSV-SARS-CoV-2 spike for 30 min (Fig. 3B, Fig. 4A ). Treating Vero cells with neutralizing antibodies to spike or with recombinant ACE2 protein prevented the activation of acid sphingomyelinase and the release of ceramide upon infection with pp-VSV-SARS-CoV-2 spike (Fig. 3B, Fig. 4A Amitriptyline and other drugs with similar structure and properties have been clinically used for many years (since 1962) to treat patients with depressive disorder. Best results were obtained with venlafaxin, fluoxetine, escitalopram and mirtazipine, drugs that were also shown in the present study to inhibit acid sphingomyelinase and ceramide release upon pp-VSV-SARS-CoV-2 spike infection.
cord-327199-ggomuomb	2014	
cord-339854-scb7pz87	2012	Vesicular stomatitis virus (VSV) is one of the most promising viruses for engineering vaccines and oncolytic therapies [2] . Of particular interest is a study in which VSV expressing the H5 antigen from highly pathogenic avian influenza induced sterilizing immunity against heterologous challenge in mice [4] . This demonstrates the safety and efficacy potential of VSV when live virus vaccination would otherwise be contraindicated. Even more promising, recombinant VSV expressing a secreted form of a virulence factor protein for Yersinia pestis, LcrV, induced high levels of LcrV-specific antibodies, protecting 90% of the mice challenged with 10 LD 50 [6] . Vesicular stomatitis virus-based Ebola vaccine is well-tolerated and protects immunocompromised nonhuman primates Potent vesicular stomatitis virus-based avian influenza vaccines provide long-term sterilizing immunity against heterologous challenge Heterologous boosting of recombinant adenoviral prime immunization with a novel vesicular stomatitis virus-vectored tuberculosis vaccine SARS vaccine based on a replicationdefective recombinant vesicular stomatitis virus is more potent than one based on a replication-competent vector
cord-345299-4k7qymqd	2020	To identify drugs that are potentially used for the treatment of COVID-19, the potency of 1403 FDA-approved drugs were evaluated using a robust pseudovirus assay and the candidates were further confirmed by authentic SARS-CoV-2 assay. Four compounds, Clomiphene (citrate), Vortioxetine, Vortioxetine (hydrobromide) and Asenapine (hydrochloride), showed potent inhibitory effects in both pseudovirus and authentic virus assay. In this study, the anti-SARS-Cov-2 potentiality of 1403 FDA approved drugs were quantitatively evaluated by the pseudovirus-based assay. In the second round of screening, inhibition of VSV-SARS-CoV-2-Sdel18 virus infection and cell cytotoxicity were both detected (Supplementary Figure 1) . The robust assay based on VSV-SARS-CoV-2-Sdel18 pseudovirus screened out the potential drugs with high efficiency, then the inhibitory effect was confirmed by authentic SARS-CoV-2 assay. The relative value or inhibition rate of candidate drugs were calculated according to the decrease of GFP positive cell number (for pseudovirus-based assay) or cytopathic effect (for authentic SARS-CoV-2-based assay).
cord-346554-a98pjtxs	2016	
cord-346777-zmmnn9b2	2019	
cord-351881-qea4b0i5	2016