A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Leninskie Gory 1-40, Moscow 119991, Russia.
Virology. 2010 Mar 1;398(1):49-56. doi: 10.1016/j.virol.2009.11.039. Epub 2009 Dec 16.
Many glycoproteins of enveloped viruses are known to be "palmitoylated" at cysteines located either in the transmembrane region or in the cytoplasmic tail. Although it was recognized early on that "palmitoylation" is not specific for this carbon chain, the exact fatty acid composition of S-acylated proteins has been difficult to determine. Advancements in mass-spectrometry (MS) now allow one to quantify the fatty acids linked to single acylation sites. We report that G of Vesicular Stomatitis virus contains palmitate at a cytoplasmic cysteine, whereas F of Newcastle Disease virus and E1 of Semliki Forest virus (SFV) are stoichiometrically acylated with stearate at a transmembrane cysteine. E2 of SFV contains three molecules of palmitate and one molecule of stearate, the latter probably attached to a transmembrane cysteine. Thus, site-specific attachment of palmitate or stearate, previously described only for HA of influenza virus, is a common feature of viral spike proteins.
许多包膜病毒的糖蛋白已知在位于跨膜区或细胞质尾部的半胱氨酸上被“棕榈酰化”。尽管早期就认识到“棕榈酰化”不是这种碳链的特异性，但 S-酰化蛋白的确切脂肪酸组成一直难以确定。质谱（MS）的进步现在允许人们定量连接到单个酰化位点的脂肪酸。我们报告称，水疱性口炎病毒的 G 蛋白在细胞质半胱氨酸上含有棕榈酸，而新城疫病毒的 F 蛋白和 Semliki Forest 病毒（SFV）的 E1 蛋白在跨膜半胱氨酸上与硬脂酸以化学计量比酰化。SFV 的 E2 含有三个棕榈酸分子和一个硬脂酸分子，后者可能附着在跨膜半胱氨酸上。因此，以前仅在流感病毒的 HA 中描述的棕榈酸或硬脂酸的位点特异性附着是病毒刺突蛋白的共同特征。
