S acylation of the hemagglutinin of influenza viruses: Mass spectrometry reveals site-specific attachment of stearic acid to a transmembrane cysteine
S acylation of the hemagglutinin of influenza viruses: Mass spectrometry reveals site-specific attachment of stearic acid to a transmembrane cysteine
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DOI：
10.1128/jvi.00704-08
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发表时间：
2008-09-01
影响因子：
5.4
通讯作者：
Veit, Michael
中科院分区：
文献类型：
--
作者：
Kordyukova, Larisa V.;Serebryakova, Marina V.;Veit, Michael
位于流感病毒血凝素 (HA) 跨膜和/或细胞质区域的半胱氨酸的 S 酰化有助于病毒粒子的膜融合和组装。我们使用质谱（MS）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的HA-酯酶融合糖蛋白是硬脂酰化的。具有一次跨膜和两个细胞质半胱氨酸的甲型流感病毒的HA同时含有棕榈酸盐和硬脂酸盐。对删除了单个半胱氨酸的重组病毒进行的 MS 分析以及串联 MS 测序揭示了令人惊讶的结果，即硬脂酸盐专门附着在位于 HA 跨膜区的半胱氨酸上。
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.