Rose J K, Bergmann J E
Cell. 1982 Oct;30(3):753-62. doi: 10.1016/0092-8674(82)90280-x.
A cDNA clone of the mRNA encoding the glycoprotein (G) of vesicular stomatitis virus was inserted into plasmid vectors under the control of either the SV40 early promoter (pSV2G) or the SV40 late promoter (pSVGL). Synthesis of G protein was observed in mouse L cells injected with pSV2G DNA or in COS1 cells transfected with pSVGL DNA. Immunofluorescent staining of G protein produced in both cell types showed a pattern of internal and cell-surface staining indistinguishable from that seen in cells infected with vesicular stomatitis virus. The G protein produced in transfected COS1 cells was the size of normal G protein and was glycosylated. Expression of a G protein lacking 79 amino acids from the COOH terminus was also examined. This G protein lacks the transmembrane domain and the hydrophilic COOH terminus, which, we postulated, anchor G protein in the lipid bilayer. This "anchorless" protein is glycosylated and is secreted, albeit slowly.
将编码水疱性口炎病毒糖蛋白（G）的mRNA的cDNA克隆插入到受SV40早期启动子（pSV2G）或SV40晚期启动子（pSVGL）控制的质粒载体中。在注射了pSV2G DNA的小鼠L细胞或用pSVGL DNA转染的COS1细胞中观察到了G蛋白的合成。两种细胞类型中产生的G蛋白的免疫荧光染色显示，其细胞内和细胞表面染色模式与感染水疱性口炎病毒的细胞中所见的模式无法区分。在转染的COS1细胞中产生的G蛋白具有正常G蛋白的大小并且进行了糖基化。还检测了一种从COOH末端缺失79个氨基酸的G蛋白的表达。这种G蛋白缺乏跨膜结构域和亲水性COOH末端，我们推测这两个结构域将G蛋白锚定在脂质双层中。这种“无锚定”蛋白进行了糖基化并且被分泌，尽管分泌速度较慢。
