A Mutant H3N2 Influenza Virus Uses an Alternative Activation Mechanism in TMPRSS2 Knockout Mice by Loss of an Oligosaccharide in the Hemagglutinin Stalk Region
A Mutant H3N2 Influenza Virus Uses an Alternative Activation Mechanism in TMPRSS2 Knockout Mice by Loss of an Oligosaccharide in the Hemagglutinin Stalk Region
复制标题
DOI：
10.1128/jvi.00124-15
复制
发表时间：
2015-05-01
影响因子：
5.4
通讯作者：
Takeda, Makoto
中科院分区：
文献类型：
--
作者：
Sakai, Kouji;Sekizuka, Tsuyoshi;Takeda, Makoto
宿主蛋白酶TMPRSS 2在具有单碱基切割位点的甲型流感病毒（IAV）血凝素（HA）蛋白的蛋白水解活化中起重要作用。然而，在TMPRSS 2敲除小鼠中传代后，H3 N2亚型IAV开始经历HA的切割活化，由于HA茎区中位置8处的寡糖的丢失，在小鼠中显示出高毒力。因此，H3 N2 IAV通过替代的HA活化机制/蛋白酶获得可切割性。
The host protease TMPRSS2 plays an essential role in proteolytic activation of the influenza A virus (IAV) hemagglutinin (HA) protein possessing a monobasic cleavage site. However, after passages in TMPRSS2 knockout mice, an H3N2 subtype IAV began to undergo cleavage activation of HA, showing high virulence in the mice due to the loss of an oligosaccharide at position 8 in the HA stalk region. Thus, the H3N2 IAV acquired cleavability by an alternative HA activation mechanism/protease(s).