The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D.
| Publication Type | Academic Article |
| Authors | Stiles K, Milne R, Cohen G, Eisenberg R, Krummenacher C |
| Journal | Virology |
| Volume | 373 |
| Issue | 1 |
| Pagination | 98-111 |
| Date Published | 02/20/2008 |
| ISSN | 0042-6822 |
| Keywords | Cell Adhesion Molecules, Down-Regulation, Herpesvirus 1, Human, Receptors, Virus, Viral Envelope Proteins |
| Abstract | 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. |
| PubMed ID | 18076965 |
| PubMed Central ID | PMC536050 |