Intercellular trafficking of herpes simplex virus type 2 UL14 deletion mutant proteins.
Intercellular trafficking of herpes simplex virus type 2 UL14 deletion mutant proteins.
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DOI：
10.1016/s0006-291x(02)02452-x
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发表时间：
2002-11
影响因子：
3.1
通讯作者：
Y. Yamauchi;F. Goshima;T. Yoshikawa;N. Nozawa;T. Koshizuka;Y. Nishiyama
中科院分区：
文献类型：
--
作者：
Y. Yamauchi;F. Goshima;T. Yoshikawa;N. Nozawa;T. Koshizuka;Y. Nishiyama
单纯疱疹病毒的 UL14 基因产物是一种在感染后期表达的 32kDa 蛋白质，是病毒粒子外皮的次要成分。我们最近证明野生型 UL14 蛋白具有热休克蛋白 (HSP) 样和/或分子伴侣样功能。在本研究中，通过免疫荧光检查转染细胞中 UL14 野生型和缺失突变蛋白的细胞内定位。我们发现，N 末端缺失突变蛋白在转染的 Vero 细胞中显示出大量细胞质、多细胞染色，而野生型/C 末端缺失突变蛋白则不然。通过使细胞在 43°C 下进行热休克，这种效果会大大增强，而用微丝破坏药物细胞松弛素 D 处理会阻碍这种效果。热休克后 UL14 抗原阳性细胞的染色模式表明该蛋白质在细胞间扩散。尽管机制尚不清楚，但这种现象似乎是一种前所未有的细胞间运输类型。
The UL14 gene product of herpes simplex virus is a 32kDa protein expressed late in infection and is a minor component of the virion tegument. We recently showed that the wild-type UL14 protein has heat shock protein (HSP)-like and/or molecular chaperone-like functions. In this study, the intracellular localization of UL14 wild-type and deletion mutant proteins was examined in transfected cells by immunofluorescence. We found that N-terminus deleted but not wild-type/C-terminus deleted mutant proteins showed a significant number of cytoplasmic, multi-cellular stains in transfected Vero cells. The effect was greatly intensified by subjecting cells to heat shock at 43°C, whereas it was obstructed by treatment with the microfilament-disrupting drug cytochalasin D. The staining patterns of UL14 antigen-positive cells after heat shock suggested a cell-to-cell spread of the protein. Although the mechanism is unclear, the phenomenon seems to be an unprecedented type of intercellular trafficking.