AI Article Synopsis

  • A novel influenza A virus subtype H17N10 was identified in little yellow-shouldered bats, featuring a unique neuraminidase (NA) gene that led to its classification as a new subtype, N10.
  • X-ray crystallography revealed the structure of the N10 NA proteins, showing similarities to other influenza NA structures but significant differences in the active site and amino acid composition, indicating potential functional divergence.
  • Due to these structural anomalies and its low enzymatic activity, researchers suggest the N10 protein should be referred to as an NA-like protein until further functional studies can clarify its role.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3503178PMC
http://dx.doi.org/10.1073/pnas.1212579109DOI Listing

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