期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 46, 页码 18903-18908出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1212579109
关键词
enzyme; mechanism; receptor; glycoprotein; infection
资金
- National Institutes of Health (NIH) [AI058113]
- Skaggs Institute for Chemical Biology
- DOE Office of Biological and Environmental Research
- NIH National Center for Research Resources, Biomedical Technology Program [P41RR001209]
- National Institute of General Medical Sciences
- National Cancer Institute [Y1CO-1020]
- National Institute of General Medical Sciences [Y1-GM-1104]
- DOE, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357, W-31-109-Eng-38]
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 angstrom and 2.5 angstrom resolution and A/little yellow-shouldered bat/Guatemala/060/2010 (GU10-060) at 2.0 angstrom. 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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