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Structural Basis of Broad Neutralization of Viral Pathogens
Author(s) -
Wilson Ian
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.484.1
Subject(s) - virology , biology , antibody , immune escape , neutralization , immune system , human immunodeficiency virus (hiv) , viral envelope , virus , immunology
Ian A. Wilson, Department of Integrative Structural and Computational Biology
The Scripps Research Institute, La Jolla, CA 92037 USA. HIV‐1, Influenza, and Hepatitis C viruses constitute significant threats to global health. These viruses are all highly variable and provide challenges to our immune system to find solutions to prevent infection against the diverse strains and subtypes of these viruses. Increasing our knowledge of how the human immune system can respond to infection by these viruses can aid in design of novel vaccines. Recently, many human antibodies have been identified that can broadly neutralize HIV‐1 and influenza viruses through binding to functionally conserved sites, such as the receptor binding site or the fusion domain. My laboratory has determined atomic structures of a wide range of broadly neutralizing antibodies in complex with the envelope proteins of HIV‐1, influenza and hepatitis C viruses. This structural information is now being used in structure‐assisted vaccine design for HIV‐1 and HCV, and for design of a more universal flu vaccine. IAW is supported by NIH grants AI100663, AI082362, AI84817, AI099275 and GM094586 and the Crucell Vaccine Institute.