PROTEIN COUNTERPARTS OF HUMAN AND SIMIAN CYTOMEGALOVIRUSES
PROTEIN COUNTERPARTS OF HUMAN AND SIMIAN CYTOMEGALOVIRUSES
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DOI：
10.1016/0042-6822(83)90265-9
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发表时间：
1983-01-01
期刊：
影响因子：
3.7
通讯作者：
GIBSON, W
中科院分区：
文献类型：
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作者：
GIBSON, W
比较了人(HCMV)和猴(SCMV)两个分离株的巨细胞病毒(CMV)蛋白。分析了三类：即刻早期(IE)蛋白、病毒颗粒中不存在的其他感染细胞特异性蛋白和构成成熟的胞外病毒粒子的蛋白。比较的基础是变性聚丙烯酰胺凝胶中的一维和二维(电荷大小)分离，以及[~(32)P]正磷酸和[~3H]氨基葡萄糖生物合成放射性标记的选择性。结果表明，大多数(如果不是全部)被识别的HCMV和SCMV蛋白在Colburn株中有对应的蛋白。作为一个群体，猿猴菌株表现出与人类菌株不同的蛋白质相似性。其中最具诊断性的是205K和145K病毒粒子蛋白，每一种都是.apprx。7K比其对应的巨细胞病毒小，以及主要的IE蛋白，比其对应的巨细胞病毒大10K-20K(取决于毒株)。科尔本菌株的蛋白质被证明更像是猿猴分离株的蛋白质，而不是恒河猴的蛋白质。使用科尔本菌株的实验提供的线索有助于鉴定一种以前未被识别的丰富的病毒粒子蛋白，它是体内和体外的主要磷酸盐受体。在HCMV病毒粒子中还发现了另外三种磷酸化蛋白，以及三种糖蛋白。通过在含有十二烷基硫酸钠的聚丙烯酰胺凝胶中的分离，仅检测到2种不同株的HCMV特异性蛋白质的差异，其中一种是Towne和Davis株的IE蛋白，另一种是AD169株的病毒衣壳蛋白。
Cytomegalovirus (CMV) proteins from isolates of both human (HCMV) and simian (SCMV) origin were compared. Three classes were analyzed: the immediate-early (IE) proteins, other infected-cell-specific proteins not present in virus particles and the proteins that constitute the mature extracellular virion. Comparisons were based on 1- and 2-dimensional (charge-size) separations in denaturing polyacrylamide gels, and on the selectivity of biosynthetic radiolabeling with [32P]orthophosphate and [3H]glucosamine. Results indicate that most, if not all, of the HCMV and SCMV proteins recognized, have counterparts in strain Colburn. As a group, the simian strains exhibit protein similarities that distinguish them from the human strains. Among the most diagnostic of these are the 205K and 145K virion proteins, each of which is .apprx. 7K smaller than its HCMV counterpart, and the predominant IE proteins, which are 10K-20K (depending upon the strain) larger than their HCMV counterparts. The proteins of strain Colburn are shown to be more like those of the simian isolates that the human, and more like those of a vervet strain than rhesus. Leads provided by experiments using strain Colburn have aided in the identification of a previously unrecognized, abundant virion protein that is a principal phosphate acceptor, both in vivo and in vitro. Three additional phosphorylated proteins are identified in HCMV virions, as well as 3 glycoproteins. Only 2 HCMV strain-specific protein differences were detected by comparisons based on separation in sodium dodecyl sulfate-containing polyacrylamide gels, one in the IE protein of strains Towne and Davis; the other in a virus capsid protein of strain AD169.