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 Angstrom resolution. This antibody and another which has only 56% s
equence 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 demonstrat
es that there is a definite flexibility in the selection of antibodies that
bind to a given epitope, despite the high affinity of their complexes. Thi
s 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.