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Structural evidence for recognition of a single epitope by two distinct antibodies
Author(s) -
Fleury Damien,
Daniels Rod S.,
Skehel John J.,
Knossow Marcel,
Bizebard Thierry
Publication year - 2000
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/1097-0134(20000901)40:4<572::aid-prot30>3.0.co;2-n
Subject(s) - epitope , antibody , complementarity determining region , complementarity (molecular biology) , biology , hemagglutinin (influenza) , virology , linear epitope , computational biology , chemistry , immunoglobulin light chain , genetics
The structure of a complex between the hemagglutinin of influenza virus and the Fab of a neutralizing antibody was determined by X‐ray crystallography at 2.8 Å resolution. This antibody and another which has only 56% sequence identity bind to the same epitope with very similar affinities and in the same orientation. One third of the interactions is conserved in the two complexes; a significant proportion of the interactions that differ are established by residues of the H3 complementarity‐determining regions (CDR) which adopt distinct conformations in the two antibodies. This demonstrates that there is a definite flexibility in the selection of antibodies that bind to a given epitope, despite the high affinity of their complexes. This flexibility allows the humoral immune response to be redundant, a feature that may be useful in achieving longer lasting protection against evolving viral pathogens. Proteins 2000;40:572–578. © 2000 Wiley‐Liss, Inc.