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-Structure paper
タイトル | West Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibody. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 103, Issue 33, Page 12400-12404, Year 2006 |
掲載日 | 2006年8月15日 |
![]() | Bärbel Kaufmann / Grant E Nybakken / Paul R Chipman / Wei Zhang / Michael S Diamond / Daved H Fremont / Richard J Kuhn / Michael G Rossmann / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 14.5 Å |
構造データ | ![]() EMDB-1234: |
由来 |
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