The vaccinia virus 39-kDa protein forms a stable complex with the p4a/4a major core protein early in morphogenesis
The vaccinia virus 39-kDa protein forms a stable complex with the p4a/4a major core protein early in morphogenesis
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DOI：
10.1006/viro.1999.0046
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发表时间：
1999-12-20
期刊：
影响因子：
3.7
通讯作者：
Rodríguez, D
中科院分区：
文献类型：
--
作者：
Risco, C;Rodríguez, JR;Rodríguez, D
痘苗病毒(VV)39-kDa蛋白是A4L基因的产物，是一种高度抗原性的病毒核心蛋白。脉冲追逐和免疫沉淀实验表明，39 kDa的蛋白与P4A(由A10L基因编码)相互作用，P4A是最丰富的病毒粒子蛋白的前体。这种相互作用与病毒粒子成熟过程中出现的经过处理的4a形式保持不变。对成熟病毒颗粒的受控破坏表明，39-kDa和4a蛋白紧密结合在病毒粒子内。免疫电子显微镜显示，这两种蛋白质首先定位在细胞质内，然后在病毒工厂内积累，通过一种显然与细胞膜无关的机制到达这些位置。双标记实验表明，这两种蛋白质在所有病毒诱导的结构中都是共存的。(C)1999年学术出版社。
The vaccinia virus (VV) 39-kDa protein, the product of the A4L gene, is a highly antigenic protein of the viral core. Pulse-chase and immunoprecipitation experiments have shown that the 39-kDa protein interacts with p4a (encoded by the A10L gene), the precursor of the most abundant virion protein. This interaction is maintained with the processed 4a form that arises during virion maturation. The controlled disruption of mature viral particles showed that the 39-kDa and 4a proteins are tightly bound within the virion. Immunoelectron microscopy showed that both proteins first localize within the cytoplasm and later accumulate inside the viral factories, reaching these locations via a mechanism apparently unrelated to cellular membranes. Double labeling experiments showed a colocalization of both proteins in all virus-induced structures. (C) 1999 Academic Press.