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Quasispecies of the D225G Substitution in the Hemagglutinin of Pandemic Influenza A(H1N1) 2009 Virus from Patients with Severe Disease in Hong Kong, China. (J Infect Dis., abstract, edited)
[Source: US National Library of Medicine, (LINK). Edited.]
J Infect Dis. 2010 Apr 2. [Epub ahead of print]
Quasispecies of the D225G Substitution in the Hemagglutinin of Pandemic Influenza A(H1N1) 2009 Virus from Patients with Severe Disease in Hong Kong, China.
Chen H, Wen X, To KK, Wang P, Tse H, Chan JF, Tsoi HW, Fung KS, Tse CW, Lee RA, Chan KH, Yuen KY. - State Key Laboratory for Emerging Infectious Diseases, 2Department of Microbiology, and 3Research Centre of Infection and Immunology, University of Hong Kong, 4Department of Pathology, United Christian Hospital, 5Department of Pathology, Kwong Wah Hospital, and 6Department of Clinical Pathology, Pamela Youde Nethersole Eastern Hospital, Hong Kong Special Administrative Region, China.
The D225G (aspartic acid to glycine) substitution in the hemagglutinin of H1N1 influenza virus may alter its receptor-binding specificity. Direct analysis of polymorphisms in 126 amino acids spanning the receptor-binding site in the hemagglutinin of pandemic H1N1 2009 virus from 117 clinical specimens in Hong Kong found the D225G substitution for 7 (12.5%) of 57 patients with severe disease and for 0 (0%) of 60 patients with mild disease. D225G quasispecies were identified mainly in endotracheal aspirate samples and were identified less frequently in nasopharyngeal aspirate samples from patients with severe disease. Continuous monitoring of the prevalence and tissue tropism of this variant during its circulation among humans is important.
PMID: 20367331 [PubMed - as supplied by publisher]
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[Source: US National Library of Medicine, (LINK). Edited.]
J Infect Dis. 2010 Apr 2. [Epub ahead of print]
Quasispecies of the D225G Substitution in the Hemagglutinin of Pandemic Influenza A(H1N1) 2009 Virus from Patients with Severe Disease in Hong Kong, China.
Chen H, Wen X, To KK, Wang P, Tse H, Chan JF, Tsoi HW, Fung KS, Tse CW, Lee RA, Chan KH, Yuen KY. - State Key Laboratory for Emerging Infectious Diseases, 2Department of Microbiology, and 3Research Centre of Infection and Immunology, University of Hong Kong, 4Department of Pathology, United Christian Hospital, 5Department of Pathology, Kwong Wah Hospital, and 6Department of Clinical Pathology, Pamela Youde Nethersole Eastern Hospital, Hong Kong Special Administrative Region, China.
The D225G (aspartic acid to glycine) substitution in the hemagglutinin of H1N1 influenza virus may alter its receptor-binding specificity. Direct analysis of polymorphisms in 126 amino acids spanning the receptor-binding site in the hemagglutinin of pandemic H1N1 2009 virus from 117 clinical specimens in Hong Kong found the D225G substitution for 7 (12.5%) of 57 patients with severe disease and for 0 (0%) of 60 patients with mild disease. D225G quasispecies were identified mainly in endotracheal aspirate samples and were identified less frequently in nasopharyngeal aspirate samples from patients with severe disease. Continuous monitoring of the prevalence and tissue tropism of this variant during its circulation among humans is important.
PMID: 20367331 [PubMed - as supplied by publisher]
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