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Title
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Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus.
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Authors
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A.T.Baker,
J.N.Varghese,
W.G.Laver,
G.M.Air,
P.M.Colman.
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Ref.
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Proteins, 1987,
2,
111-117.
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PubMed id
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Abstract
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Neuraminidases from different subtypes of influenza virus are characterized by
the absence of serological cross-reactivity and an amino acid sequence homology
of approximately 50%. The three-dimensional structure of the neuraminidase
antigen of subtype N9 from an avian influenza virus (A/tern/Australia/G70c/75)
has been determined by X-ray crystallography and shown to be folded similarly to
neuraminidase of subtype N2 isolated from a human influenza virus. This result
demonstrates that absence of immunological cross-reactivity is no measure of
dissimilarity of polypeptide chain folding. Small differences in the way in
which the subunits are organized around the molecular fourfold axis are
observed. Insertions and deletions with respect to subtype N2 neuraminidase
occur in four regions, only one of which is located within the major antigenic
determinants around the enzyme active site.
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