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INFLUENZA VIRUS HEMAGGLUTININ, (ESCAPE) MUTANT WITH THR 131 REPLACED BY ILE, COMPLEXED WITH A NEUTRALIZING ANTIBODYINFLUENZA VIRUS HEMAGGLUTININ, (ESCAPE) MUTANT WITH THR 131 REPLACED BY ILE, COMPLEXED WITH A NEUTRALIZING ANTIBODY
Structural highlights
FunctionEvolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of the hemagglutinin (HA) of a mutant influenza virus that escapes neutralization by a monoclonal antibody shows that the mutation causes changes in HA structure which avoid an energetically less favorable conformation. However, the structure of the mutant HA.Fab complex indicates that the antibody binds selectively to mutant HA in a wild type-like distorted conformation. The association of an antibody with a less favored HA conformation represents an alternative to previously described mechanisms of escape from neutralization by antibodies. Antigen distortion allows influenza virus to escape neutralization.,Fleury D, Wharton SA, Skehel JJ, Knossow M, Bizebard T Nat Struct Biol. 1998 Feb;5(2):119-23. PMID:9461077[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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