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TitleWest Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibody.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 103, Issue 33, Page 12400-12404, Year 2006
Publish dateAug 15, 2006
AuthorsBärbel Kaufmann / Grant E Nybakken / Paul R Chipman / Wei Zhang / Michael S Diamond / Daved H Fremont / Richard J Kuhn / Michael G Rossmann /
PubMed AbstractFlaviviruses, 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 ...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-Angstrom 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 E16 antibody neutralizes WNV by blocking the initial rearrangement of the E glycoprotein before fusion with a cellular membrane.
External linksProc Natl Acad Sci U S A / PubMed:16895988 / PubMed Central
MethodsEM (single particle)
Resolution14.5 Å
Structure data

EMDB-1234:
West Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibody.
Method: EM (single particle) / Resolution: 14.5 Å

Source
  • unidentified (others)

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