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Structural basis of West Nile virus neutralization by a therapeutic antibody

Author

Listed:
  • 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
    Washington University School of Medicine
    Washington University School of Medicine)

  • Daved H. Fremont

    (Washington University School of Medicine
    Washington University School of Medicine)

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.

Suggested Citation

  • Grant E. Nybakken & Theodore Oliphant & Syd Johnson & Stephen Burke & Michael S. Diamond & Daved H. Fremont, 2005. "Structural basis of West Nile virus neutralization by a therapeutic antibody," Nature, Nature, vol. 437(7059), pages 764-769, September.
    • Handle: RePEc:nat:nature:v:437:y:2005:i:7059:d:10.1038_nature03956
    DOI: 10.1038/nature03956
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    Cited by:

    1. Aroop Sircar & Jeffrey J Gray, 2010. "SnugDock: Paratope Structural Optimization during Antibody-Antigen Docking Compensates for Errors in Antibody Homology Models," PLOS Computational Biology, Public Library of Science, vol. 6(1), pages 1-13, January.
    2. Arun V. Iyer & Konstantin G. Kousoulas, 2013. "A Review of Vaccine Approaches for West Nile Virus," IJERPH, MDPI, vol. 10(9), pages 1-24, September.

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