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Title
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Structure of influenza virus haemagglutinin complexed with a neutralizing antibody.
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Authors
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T.Bizebard,
B.Gigant,
P.Rigolet,
B.Rasmussen,
O.Diat,
P.Bösecke,
S.A.Wharton,
J.J.Skehel,
M.Knossow.
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Ref.
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Nature, 1995,
376,
92-94.
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PubMed id
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Abstract
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Haemagglutinin (HA) is the influenza surface glycoprotein that interacts with
infectivity-neutralizing antibodies. As a consequence of this immune pressure,
it is the variable virus component, which is important in antigenic drift, that
results in recurrent epidemics of influenza. We have determined the
crystallographic structure of a complex formed between the antigen-binding
fragment (Fab) of a neutralizing antibody and the membrane-distal domain ('HA
top') of a HA subunit prepared from HA in its membrane-fusion-active
conformation. A dramatic change is seen in the structure of the Fab-combining
site on complex formation. Our results indicate that neutralization of
infectivity by this antibody involves the inhibition of receptor binding, and
demonstrate how influenza virus can maintain its conserved receptor-binding site
despite the immune selective pressure for change in this region of the molecule;
they also contribute to a complete description of the endosomal pH-induced
fusion-active HA structure.
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