West Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibody

Bärbel Kaufmann, Grant E. Nybakken, Paul R. Chipman, Wei Zhang, Michael S. Diamond, Daved H. Fremont, Richard J. Kuhn, Michael G. Rossmann

Research output: Contribution to journalArticlepeer-review

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Flaviviruses, such as West Nile virus (WNV), are significant human pathogens. The humoral immune response plays an important role in the control of flavivirus infection and disease. The structure of WNV complexed with the Fab fragment of the strongly neutralizing mAb E16 was determined to 14.5-Å resolution with cryo-electron microscopy. E16, an antibody with therapeutic potential, binds to domain III of the WNV envelope glycoprotein. Because of steric hindrance, Fab E16 binds to only 120 of the 180 possible binding sites on the viral surface. Fitting of the previously determined x-ray structure of the Fab-domain III complex into the cryo-electron microscopy density required a change of the elbow angle between the variable and constant domains of the Fab. The structure suggests that the E1G antibody neutralizes WNV by blocking the initial rearrangement of the E glycoprotein before fusion with a cellular membrane.

Original languageEnglish (US)
Pages (from-to)12400-12404
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number33
StatePublished - Aug 15 2006


  • Cryo-electron microscopy
  • Flavivirus
  • Neutralization


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