Maurer-Stroh Sebastian, Lee Raphael Tze Chuen, Eisenhaber Frank, Cui Lin, Phuah Shiau Pheng, Lin Raymond Tp
Bioinformatics Institute (BII), ASTAR Singapore; Bioinformatics Institute (BII), A*STAR; Bioinformatics Institute (BII) A*STAR Singapore and National Public Health Laboratory, Ministry of Health, Singapore.
PLoS Curr. 2010 Jun 1;2:RRN1162. doi: 10.1371/currents.rrn1162.
As the 2009 (H1N1) influenza A virus continues evolving, most mutations appear geographically and temporally confined. However, the latest surveillance data suggests emergence of a new prominent mutation, E391K, in the hemagglutinin (HA) that is globally on the rise. Interestingly, when modelled in the context of the available HA crystal structure, this mutation could alter salt bridge patterns and stability in a region of the HA oligomerization interface that is important for membrane fusion and also a known antigenic site. We discuss occurrence of HA-E391K in global surveillance data and associated clinical phenotypes from Singapore ranging from mostly mild to few severe symptoms, including sporadic vaccine failure. More clinical and experimental data are needed to determine if this mutation could alter the biology and fitness of the virus or if its increased occurrence is due to founder effects.
随着2009年甲型H1N1流感病毒不断演变，多数突变在地理和时间上似乎受到限制。然而，最新监测数据表明，血凝素（HA）中出现了一种新的显著突变E391K，且在全球范围内呈上升趋势。有趣的是，根据现有的HA晶体结构进行模拟时，这种突变可能会改变HA寡聚化界面区域的盐桥模式和稳定性，该区域对膜融合很重要，也是一个已知的抗原位点。我们讨论了全球监测数据中HA-E391K的出现情况以及新加坡相关的临床表型，这些表型从大多为轻症到少数重症症状不等，包括偶发的疫苗接种失败。需要更多的临床和实验数据来确定这种突变是否会改变病毒的生物学特性和适应性，或者其发生率增加是否是由于奠基者效应。
