key: cord-0035901-oxwtxlm8
authors: Georgiev, Vassil St.
title: Virology
date: 2009
journal: National Institute of Allergy and Infectious Diseases, NIH
DOI: 10.1007/978-1-60327-297-1_7
sha: 54be80a0ce444a095008a5784be934e074593996
doc_id: 35901
cord_uid: oxwtxlm8

NIAD supports a broad spectrum of both basic and applied research in virology to expand the understanding of the biology, pathogenesis, and the immunology of viral diseases, leading to their prevention, control, and treatment, including research on (i) the viral replication cycle; (ii) the structure and function of the viral components; (iii) host virus interactions, including pathogenesis, immune evasion, and immune enhancement; (iv) viral genetics and evolution; (v) viral interference and defective interfering particles; (vi) virus vector relationships; (vii) epidemiology and natural history; and (viii) preclinical and clinical research to develop vaccines, adjuvants, therapeutics, immunomodulators, and diagnostics (http://www3.niaid.nih.gov/research/topics/viral/introduction.)

The most important task of the NIAID Antiviral Testing Program is the evaluation of the efficacy and toxicity of new antiviral agents using a broad array of in vitro assays and in vivo animal models (http://www3.niaid.nih.gov/ research/topics/viral/resources.htm). The main objective of this program is to identify antiviral agents with the potential to treat viral infections of public health importance, including those for newly emerging infections and those that are not a high priority for the pharmaceutical industry. NIAID ensures that the intellectual property rights of the compound supplier are protected. The viruses and models covered under this program include:

In Vitro Screens r Herpesviruses: herpes simplex virus-1 (HSV-1); herpes For the paramyxoviruses, the fusion (F) protein catalyzes this membrane merger and entry step, and it has been postulated that the F protein undergoes complex refolding during this process. The crystal structure of the parainfluenza virus 5 F protein in its prefusion conformation and stabilized by the addition of a carboxy-terminal trimerization domain has been elucidated (2) . The positions and structural transitions of key parts of the fusion machinery, including the hydrophobic fusion peptide and two helical heptad repeat regions, clarified the mechanism of the F protein-mediated membrane fusion. 

Insulin degrading enzyme is a cellular receptor mediating varicella-zoster virus infection and cell-to-cell spread

Structure of the parainfluenza virus 5 F protein in its metastable, prefusion confirmation

Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus