Nuclear sequestration of cellular chaperone and proteasomal machinery during herpes simplex virus type 1 infection
Nuclear sequestration of cellular chaperone and proteasomal machinery during herpes simplex virus type 1 infection
复制标题
DOI：
10.1128/jvi.78.13.7175-7185.2004
复制
发表时间：
2004-07-01
影响因子：
5.4
通讯作者：
Weller, SK
中科院分区：
文献类型：
--
作者：
Burch, AD;Weller, SK
1 型单纯疱疹病毒 (HSV-1) 编码一种门户蛋白，该蛋白形成大型寡聚结构，据信为 DNA 进出衣壳提供通道。伴侣蛋白通常促进此类复杂结构的折叠和多聚化。在这份报告中，我们表明细胞伴侣蛋白、26S 蛋白酶体的成分和泛素缀合蛋白被隔离在受感染细胞核中的离散病灶中。早期病毒蛋白 ICP0 被证明是在感染早期建立这些病灶所必需的，并且足以在转染细胞中重新分配伴侣分子。此外，我们发现，在感染过程中，门户蛋白 UL6 不仅定位于这些位点，而且还是泛素修饰的底物。我们的结果表明，HSV-1 已经进化出一种优雅的机制，用于促进细胞核内特定灶点的蛋白质质量控制。
Herpes simplex virus type 1 (HSV-1) encodes a portal protein that forms a large oligomeric structure believed to provide the conduit for DNA entry and exit from the capsid. Chaperone proteins often facilitate the folding and multimerization of such complex structures. In this report, we show that cellular chaperone proteins, components of the 26S proteasome, and ubiquitin-conjugated proteins are sequestered in discrete foci in the nucleus of the infected cell. The immediate-early viral protein ICP0 was shown to be necessary to establish these foci at early times during infection and sufficient to redistribute chaperone molecules in transfected cells. Furthermore, we found that not only is the portal protein, UL6, localized to these sites during infection, but it is also a substrate for ubiquitin modification. Our results suggest that HSV-1 has evolved an elegant mechanism for facilitating protein quality control at specialized foci within the nucleus.