The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D.
The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D.
复制标题
单纯疱疹病毒受体 nectin-1 在与糖蛋白 D 反式相互作用后下调。
DOI:
10.1016/j.virol.2007.11.012
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发表时间:
2008
期刊:
影响因子:
3.7
通讯作者:
Krummenacher,Claude
中科院分区:
文献类型:
--
作者:
Stiles,KatieM;Milne,RichardSB;Cohen,GaryH;Eisenberg,RoselynJ;Krummenacher,Claude
During herpes simplex virus (HSV) entry, membrane fusion occurs either on the cell surface or after virus endocytosis. In both cases, binding of glycoprotein D (gD) to a receptor such as nectin-1 or HVEM is required. In this study, we co-cultured cells expressing gD with nectin-1 expressing cells to investigate the effects of gD on nectin-1 at cell contacts. After overnight co-cultures with gD expressing cells, there was a down-regulation of nectin-1 in B78H1-C10, SY5Y, A431 and HeLa cells, which HSV enters by endocytosis. In contrast, on Vero cells, which HSV enters at the plasma membrane, nectin-1 was not down-regulated. Further analysis of B78H1-derived cells showed that nectin-1 down-regulation corresponds to the ability of gD to bind nectin-1 and is achieved by internalization and low-pH-dependent degradation of nectin-1. Moreover, gD is necessary for virion internalization in B78H1 cells expressing nectin-1. These data suggest that the determinants of gD-mediated internalization of nectin-1 may direct HSV to an endocytic pathway during entry.