State Key Laboratory for Emerging Infectious Diseases, University of Hong Kong, China.
J Infect Dis. 2010 May 15;201(10):1517-21. doi: 10.1086/652661.
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.
H1N1 流感病毒血凝素中的 D225G（天冬氨酸被甘氨酸取代）突变可能改变其受体结合特异性。对来自香港 117 份临床标本的大流行 H1N1 2009 病毒血凝素中跨越受体结合位点的 126 个氨基酸的多态性进行直接分析，发现 D225G 取代发生在 57 例重症患者中的 7 例（12.5%），而在 60 例轻症患者中未发现该取代。D225G 准种主要在气管吸出物样本中鉴定到，在重症患者的鼻咽吸出物样本中鉴定到的频率较低。在该变体在人群中传播期间，对其流行情况和组织嗜性进行连续监测非常重要。
