Structural evidence for recognition of a single epitope by two distinct antibodies

  • Fleury D
  • Daniels R
  • Skehel J
 et al. 
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Abstract

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 A 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.

Author-supplied keywords

  • Antibody
  • Epitope
  • Hemagglutinin
  • Influenza
  • Redundancy
  • Structure

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Authors

  • Damien Fleury

  • Rod S. Daniels

  • John J. Skehel

  • Marcel Knossow

  • Thierry Bizebard

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