Release of fatty acids from virus glycoproteins by hydroxylamine.
Release of fatty acids from virus glycoproteins by hydroxylamine.
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通过羟胺从病毒糖蛋白中释放脂肪酸。
DOI：
10.1016/0304-4165(84)90298-8
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
Schlesinger,MJ
中科院分区：
文献类型：
--
作者：
Magee,AI;Koyama,AH;Malfer,C;Wen,D;Schlesinger,MJ
辛德毕斯和水泡性口炎病毒的糖蛋白结合的脂肪酸可以通过在pH 8.0下用1 M羟胺处理蛋白质来释放，但是三种蛋白质的释放速率差异很大。最不稳定的脂肪酰基键是在辛德毕斯病毒PE 2/E2蛋白和最稳定的是在E1蛋白。辛德毕斯病毒糖蛋白中的部分脂肪酸经硼氢化钠处理后被还原为醇，表明蛋白质结合的脂肪酸可能以硫酯键连接。辛德毕斯病毒PE 2/E2在羧基末端附近有几个半胱氨酸残基，这是一个假定位于双层内部（细胞质面）的蛋白质区域，含有E2蛋白的微粒体膜的蛋白酶消化去除了一小部分细胞质尾区以及大量的脂肪酸。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和一个显着的分数的G蛋白转化为二硫键连接的二聚体由羟胺。这些数据暗示这些蛋白质上的半胱氨酰基团作为参与脂肪酸酰化的位点。
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.