Schenk P, Woods A S, Gibson W
Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
J Virol. 1991 Mar;65(3):1525-9. doi: 10.1128/JVI.65.3.1525-1529.1991.
Intranuclear B-capsids from cytomegalovirus (strain Colburn)-infected cells contain an abundant 37-kDa assembly protein, thought to be involved in capsid formation, and three minor protein constituents (i.e., 45, 39, and 38 kDa) that are immunologically and structurally related to the assembly protein. In the experiments reported here, antisera produced against synthetic peptides were used in conjunction with chemical protein cleavage to examine the structural relationship of these proteins in more detail. Results of these experiments verify that the carboxyl end of the 39-kDa assembly protein precursor is lost during maturation and suggest that the 38-kDa protein may be a processing intermediate. It is shown that the 45-kDa protein is coterminal with the mature assembly protein at its carboxyl end but differs by a predicted 115-amino-acid extension at its amino terminus. In addition, evidence is presented that the 45-kDa protein has a 48-kDa precursor and a 47-kDa putative processing intermediate which have the same carboxy-terminal sequences and undergo the same maturational events as those of the assembly protein. A working model considering the structural relationship of these proteins is presented.
来自巨细胞病毒（科尔本株）感染细胞的核内B型衣壳含有一种丰富的37 kDa组装蛋白，被认为参与衣壳形成，以及三种较小的蛋白质成分（即45、39和38 kDa），它们在免疫和结构上与组装蛋白相关。在本文报道的实验中，针对合成肽产生的抗血清与化学蛋白质裂解结合使用，以更详细地研究这些蛋白质的结构关系。这些实验结果证实，39 kDa组装蛋白前体的羧基末端在成熟过程中丢失，并表明38 kDa蛋白可能是一种加工中间体。结果表明，45 kDa蛋白在其羧基末端与成熟组装蛋白共末端，但在其氨基末端有一个预测的115个氨基酸的延伸。此外，有证据表明，45 kDa蛋白有一个48 kDa前体和一个47 kDa假定加工中间体，它们具有相同的羧基末端序列，并经历与组装蛋白相同的成熟事件。本文提出了一个考虑这些蛋白质结构关系的工作模型。
