Quasispecies of the D225G substitution in the hemagglutinin of pandemic influenza A(H1N1) 2009 virus from patients with severe disease in Hong Kong, 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.
Chen
Honglin
H
State Key Laboratory for Emerging Infectious Diseases, University of Hong Kong, China.
Wen
Xi
X
To
Kelvin K W
KK
Wang
Pui
P
Tse
Herman
H
Chan
Jasper F W
JF
Tsoi
Hoi-Wah
HW
Fung
Kitty S C
KS
Tse
Cindy W S
CW
Lee
Rodney A
RA
Chan
Kwok-Hung
KH
Yuen
Kwok-Yung
KY
D019943:Amino Acid Substitution; D004196:Disease Outbreaks; D006388:Hemagglutinins / Q000235:genetics*; D006723:Hong Kong / Q000453:epidemiology; D006801:Humans; D053118:Influenza A Virus, H1N1 Subtype / Q000235:genetics*; D007251:Influenza, Human / Q000453:epidemiology* / Q000821:virology*
D006388:Hemagglutinins