Structural basis of West Nile virus neutralization by a therapeutic antibody

Grant E. Nybakken, Theodore Oliphant, Syd Johnson, Stephen Burke, Michael S. Diamond and Daved H. Fremont ()
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Grant E. Nybakken: Washington University School of Medicine
Theodore Oliphant: Washington University School of Medicine
Syd Johnson: MacroGenics
Stephen Burke: MacroGenics
Michael S. Diamond: Washington University School of Medicine
Daved H. Fremont: Washington University School of Medicine

Nature, 2005, vol. 437, issue 7059, 764-769

Abstract: Pushing the envelope West Nile virus is closely related to the human epidemic-causing dengue, yellow fever and Japanese encephalitis viruses. The study of a particularly effective monoclonal antibody, capable of protecting mice from lethal West Nile virus challenge even if administered 5 days after infection, has provided important information on the structural basis of viral neutralization. The work highlights the domain III region of the viral envelope protein as a potential target for both therapeutic antibodies and vaccines.

Date: 2005
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DOI: 10.1038/nature03956

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