Giuseppe
Emeritus
[Source: US National Library of Medicine, full page: (LINK). Abstract, edited.]
Cell Res. 2013 Nov 12. doi: 10.1038/cr.2013.150. [Epub ahead of print]
Solving the mystery of H7N9 by crystal balls.
Yuen KY.
Source: State Key Laboratory for Emerging Infectious Diseases, Department of Microbiology, The University of Hong Kong, Pokfulam Road, Pokfulam, Hong Kong SAR, China.
Abstract
How the novel influenza H7N9 virus crossed species barrier from avian to human is intriguing. Extrapolation from previous studies on H5N1 can be misleading as illustrated by crystallographic studies on the H7 hemagglutinin with G226L substitution; crystal structure of the neuraminidase N9 showed that R294K substitution interferes with binding to sialic acid or antiviral drugs and reduces viral fitness.
PMID: 24217769 [PubMed - as supplied by publisher]
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Cell Res. 2013 Nov 12. doi: 10.1038/cr.2013.150. [Epub ahead of print]
Solving the mystery of H7N9 by crystal balls.
Yuen KY.
Source: State Key Laboratory for Emerging Infectious Diseases, Department of Microbiology, The University of Hong Kong, Pokfulam Road, Pokfulam, Hong Kong SAR, China.
Abstract
How the novel influenza H7N9 virus crossed species barrier from avian to human is intriguing. Extrapolation from previous studies on H5N1 can be misleading as illustrated by crystallographic studies on the H7 hemagglutinin with G226L substitution; crystal structure of the neuraminidase N9 showed that R294K substitution interferes with binding to sialic acid or antiviral drugs and reduces viral fitness.
PMID: 24217769 [PubMed - as supplied by publisher]
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