Davidson S K, Hunt L A
Biochem J. 1985 Jul 1;229(1):47-55. doi: 10.1042/bj2290047.
We have examined and compared the host-cell-dependent glycosylation of the G glycoprotein of vesicular-stomatitis virus (Hazelhurst strain) and the E1 and E2 glycoproteins of Sindbis virus replicated by baby-hamster kidney, chicken-embryo fibroblast and mouse L929 monolayer cell cultures. The results of endo-beta-N-acetylglucosaminidase H digestion of viral proteins labelled with [3H]mannose or leucine and Pronase-digested glycopeptides labelled with [3H]mannose indicated that both the G protein and the E1 protein contained a similar mixture of endoglycosidase-resistant oligosaccharides of the complex acidic type and less extensively processed endoglycosidase-sensitive oligosaccharides of the neutral or hybrid type, with a relatively greater content of the endoglycosidase-sensitive oligosaccharides for virus replicated in the chicken as against hamster or mouse cells. A large fraction of the G protein and the majority of the E1 proteins from the mammalian host cells contained acidic-type oligosaccharides at both glycosylation sites, whereas most of the G and E1 glycoproteins from the avian host cells and essentially all of the E2 protein from all three host-cell types contained an acidic-type oligosaccharide at one site and neutral- or hybrid-type oligosaccharide at the other site. The relative increase in neutral- and hybrid-type oligosaccharides with five-mannose core structures observed for the G and E1 proteins of virus released from the avian host cells suggested that two specific steps in oligosaccharide processing (mediated by alpha-mannoside II and N-acetylglucosaminyltransferase I) were less efficient at one of the glycosylation sites of the vesicular-stomatitis-virus G protein and Sindbis-virus E1 protein in the avian as against mammalian host cells.
我们检测并比较了水泡性口炎病毒（黑泽赫斯特株）的G糖蛋白以及辛德毕斯病毒的E1和E2糖蛋白在幼仓鼠肾细胞、鸡胚成纤维细胞和小鼠L929单层细胞培养物中宿主细胞依赖性糖基化情况。用[³H]甘露糖或亮氨酸标记病毒蛋白后进行内切β-N-乙酰葡糖胺糖苷酶H消化，以及用[³H]甘露糖标记经链霉蛋白酶消化的糖肽，结果表明G蛋白和E1蛋白都含有复杂酸性型内切糖苷酶抗性寡糖和加工程度较低的中性或杂合型内切糖苷酶敏感寡糖的相似混合物，与在仓鼠或小鼠细胞中复制的病毒相比，在鸡细胞中复制的病毒中内切糖苷酶敏感寡糖的含量相对更高。来自哺乳动物宿主细胞的大部分G蛋白和大部分E1蛋白在两个糖基化位点都含有酸性型寡糖，而来自禽类宿主细胞的大部分G和E1糖蛋白以及来自所有三种宿主细胞类型的基本上所有E2蛋白在一个位点含有酸性型寡糖，在另一个位点含有中性或杂合型寡糖。从禽类宿主细胞释放的病毒的G和E1蛋白中观察到具有五甘露糖核心结构的中性和杂合型寡糖相对增加，这表明在禽类宿主细胞中，与哺乳动物宿主细胞相比，寡糖加工的两个特定步骤（由α-甘露糖苷酶II和N-乙酰葡糖胺基转移酶I介导）在水泡性口炎病毒G蛋白和辛德毕斯病毒E1蛋白的一个糖基化位点效率较低。
