流感病毒血凝素的硬脂酰化：质谱分析揭示硬脂酸在跨膜半胱氨酸上的位点特异性附着。
S acylation of the hemagglutinin of influenza viruses: mass spectrometry reveals site-specific attachment of stearic acid to a transmembrane cysteine.
作者信息
Kordyukova Larisa V, Serebryakova Marina V, Baratova Ludmila A, Veit Michael
机构信息
A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119991, Russia.
出版信息
J Virol. 2008 Sep;82(18):9288-92. doi: 10.1128/JVI.00704-08. Epub 2008 Jul 2.
Abstract
S acylation of cysteines located in the transmembrane and/or cytoplasmic region of influenza virus hemagglutinins (HA) contributes to the membrane fusion and assembly of virions. Our results from using mass spectrometry (MS) show that influenza B virus HA possessing two cytoplasmic cysteines contains palmitate, whereas HA-esterase-fusion glycoprotein of influenza C virus having one transmembrane cysteine is stearoylated. HAs of influenza A virus having one transmembrane and two cytoplasmic cysteines contain both palmitate and stearate. MS analysis of recombinant viruses with deletions of individual cysteines, as well as tandem-MS sequencing, revealed the surprising result that stearate is exclusively attached to the cysteine positioned in the transmembrane region of HA.
摘要
流感病毒血凝素（HA）跨膜和/或细胞质区域中的半胱氨酸酰化作用有助于病毒粒子的膜融合和组装。我们使用质谱（MS）得到的结果表明，具有两个细胞质半胱氨酸的乙型流感病毒HA含有棕榈酸酯，而具有一个跨膜半胱氨酸的丙型流感病毒HA酯酶融合糖蛋白则被硬脂酰化。具有一个跨膜和两个细胞质半胱氨酸的甲型流感病毒HA同时含有棕榈酸酯和硬脂酸酯。对个别半胱氨酸缺失的重组病毒进行的MS分析以及串联MS测序揭示了一个惊人的结果，即硬脂酸酯仅附着于HA跨膜区域中的半胱氨酸上。
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