Magee A I, Koyama A H, Malfer C, Wen D, Schlesinger M J
Biochim Biophys Acta. 1984 Apr 10;798(2):156-66. doi: 10.1016/0304-4165(84)90298-8.
The fatty acids bound to the glycoproteins of Sindbis and vesicular stomatitis viruses can be released by treating the protein with 1 M hydroxylamine at pH 8.0, but the rates of release vary greatly among the three proteins. The most labile fatty acyl bonds were in the Sindbis virus PE2/E2 proteins and the most stable were in the E1 protein. Some of the fatty acids in Sindbis virus glycoproteins were reduced to the alcohol after treatment with sodium borohydride, indicating that protein-bound fatty acids could be in thiolester linkage. Sindbis virus PE2/E2 has several cysteine residues near the carboxy terminus, a region of the protein postulated to be localized on the inside (cytoplasmic face) of the bilayer, and protease digestion of microsomal membranes containing E2 protein removed a small portion of this cytoplasmic tail as well as significant amounts of the fatty acid. For the vesicular stomatitis virus G protein, the sensitivity of fatty acid hydrolysis appeared to depend on the conformation of the protein and a significant fraction of G protein was converted to a disulfide-linked dimer by hydroxylamine. These data implicate cysteinyl groups on these proteins as sites involved in fatty acid acylation.
辛德毕斯病毒和水泡性口炎病毒糖蛋白上结合的脂肪酸，可通过在pH 8.0条件下用1 M羟胺处理蛋白质而释放出来，但三种蛋白质的释放速率差异很大。最不稳定的脂肪酰键存在于辛德毕斯病毒的PE2/E2蛋白中，最稳定的则存在于E1蛋白中。用硼氢化钠处理后，辛德毕斯病毒糖蛋白中的一些脂肪酸被还原为醇，这表明与蛋白质结合的脂肪酸可能以硫酯键形式存在。辛德毕斯病毒PE2/E2在羧基末端附近有几个半胱氨酸残基，该区域被认为位于双层膜的内侧（细胞质面），对含有E2蛋白的微粒体膜进行蛋白酶消化，会去除一小部分这种细胞质尾巴以及大量脂肪酸。对于水泡性口炎病毒G蛋白，脂肪酸水解的敏感性似乎取决于蛋白质的构象，并且相当一部分G蛋白会被羟胺转化为二硫键连接的二聚体。这些数据表明这些蛋白质上的半胱氨酰基团是参与脂肪酸酰化的位点。
