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Crystal structures of two subtype n10 neuraminidase-like proteins from bat influenza a viruses reveal a diverged putative active site

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Overview

authors

  • Zhu, X. Y.
  • Yang, H.
  • Guo, Z.
  • Yu, W. L.
  • Carney, P. J.
  • Li, Yuxing
  • Chen, L. M.
  • Paulson, James
  • Donis, R. O.
  • Tong, S. X.
  • Stevens, J.
  • Wilson, Ian

publication date

  • November 2012

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Recently, we reported a unique influenza A virus subtype H17N10 from little yellow-shouldered bats. Its neuraminidase (NA) gene encodes a protein that appears to be highly divergent from all known influenza NAs and was assigned as a new subtype N10. To provide structural and functional insights on the bat H17N10 virus, X-ray structures were determined for N10 NA proteins from influenza A viruses A/little yellow-shouldered bat/Guatemala/164/2009 (GU09-164) in two crystal forms at 1.95 Å and 2.5 Å resolution and A/little yellow-shouldered bat/Guatemala/060/2010 (GU10-060) at 2.0 Å. The overall N10 structures are similar to each other and to other known influenza NA structures, with a single highly conserved calcium binding site in each monomer. However, the region corresponding to the highly conserved active site of influenza A N1-N9 NA subtypes and influenza B NA differs substantially. In particular, most of the amino acid residues required for NA activity are substituted, and the putative active site is much wider because of displacement of the 150-loop and 430-loop. These structural features and the fact that the recombinant N10 protein exhibits no, or extremely low, NA activity suggest that it may have a different function than the NA proteins of other influenza viruses. Accordingly, we propose that the N10 protein be termed an NA-like protein until its function is elucidated.

subject areas

  • Animals
  • Catalytic Domain
  • Chiroptera
  • Crystallography, X-Ray
  • Evolution, Molecular
  • Influenza A virus
  • Neuraminidase
  • Protein Structure, Secondary
  • Viral Proteins
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Research

keywords

  • enzyme
  • glycoprotein
  • infection
  • mechanism
  • receptor
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Identity

PubMed Central ID

  • PMC3503178

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.1212579109

PubMed ID

  • 23012478
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Additional Document Info

start page

  • 18903

end page

  • 18908

volume

  • 109

issue

  • 46

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