Chimeric influenza virus hemagglutinin containing either the NH2 terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface.
Chimeric influenza virus hemagglutinin containing either the NH2 terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface.
复制标题
含有水疱性口炎病毒G蛋白的NH2末端或COOH末端的嵌合流感病毒血凝素在转运至细胞表面方面存在缺陷。
DOI：
10.1073/pnas.81.2.395
复制
发表时间：
1984
影响因子：
11.1
通讯作者：
Compans,RW
中科院分区：
文献类型：
--
作者：
McQueen,NL;Nayak,DP;Jones,LV;Compans,RW
构建了流感病毒血凝素（HA）的嵌合cDNA克隆，其中编码HA的NH2端或COOH端的DNA被水泡性口炎病毒G蛋白的DNA取代。嵌合cdna （GHA或HAG）在CV1细胞中使用猴病毒40晚期替代启动子表达。两种嵌合蛋白都经过合成、糖基化并转运到粗内质网。这些结果表明，水疱性口炎病毒G蛋白nh2末端序列可以为易位提供信号功能，cooh末端序列可以替代流感病毒HA的类似序列，为HA提供锚定功能。然而，嵌合糖蛋白没有被运输到高尔基复合体或质膜。讨论了这些结果在转运、分拣和运输过程中的意义。
Chimeric cDNA clones of influenza virus hemagglutinin (HA) were constructed in which the DNA encoding either the NH2 terminus or the COOH terminus of HA was replaced with that of a vesicular stomatitis virus G protein. The chimeric cDNAs (GHA or HAG) were expressed in CV1 cells using the simian virus 40 late replacement promoter. Both chimeric proteins are synthesized, glycosylated, and transported to the rough endoplasmic reticulum. These results show that the NH2-terminal sequences of vesicular stomatitis virus G protein can provide a signal function for translocation and the COOH-terminal sequences can provide the anchor function for the influenza virus HA, when substituted for similar sequences. However, the chimeric glycoproteins were not transported to the Golgi complex or the plasma membrane. The implication of these results in translocation, sorting, and transport processes is discussed.