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. (C) 2000 Wiley-Liss, Inc.
CITATION STYLE
Fleury, D., Daniels, R. S., Skehel, J. J., Knossow, M., & Bizebard, T. (2000). Structural evidence for recognition of a single epitope by two distinct antibodies. Proteins: Structure, Function and Genetics, 40(4), 572–578. https://doi.org/10.1002/1097-0134(20000901)40:4<572::AID-PROT30>3.0.CO;2-N
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