Whitt M A, Rose J K
Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510.
Virology. 1991 Dec;185(2):875-8. doi: 10.1016/0042-6822(91)90563-q.
We have investigated the role of fatty acid acylation on two properties of the glycoprotein (G protein) from the Indiana serotype of vesicular stomatitis virus (VSV). Using a mutated G protein described previously (CS-2) that is not palmitylated, we found that fatty acid acylation was not required for the low pH-induced membrane fusion activity of VSV G protein. Transient expression of CS in HeLa cells resulted in syncytia formation that was indistinguishable from that induced by wild-type G protein. In addition, we found that expression of CS complemented a temperature-sensitive mutant of VSV (tsO45) as well as the wild-type protein. These results indicate that the presence of palmitate on the cytoplasmic domain of VSV G protein is not required for any step in the life cycle of the virus.
我们研究了脂肪酸酰化对水疱性口炎病毒（VSV）印第安纳血清型糖蛋白（G蛋白）两种特性的作用。使用先前描述的未被棕榈酰化的突变G蛋白（CS-2），我们发现脂肪酸酰化对于VSV G蛋白低pH诱导的膜融合活性并非必需。CS在HeLa细胞中的瞬时表达导致了合胞体形成，这与野生型G蛋白诱导的合胞体形成没有区别。此外，我们发现CS的表达补充了VSV的温度敏感突变体（tsO45）以及野生型蛋白。这些结果表明，VSV G蛋白胞质结构域上棕榈酸的存在对于病毒生命周期的任何步骤都不是必需的。
