Glycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entry.
| Publication Type | Academic Article |
| Authors | Stiles K, Krummenacher C |
| Journal | Virology |
| Volume | 399 |
| Issue | 1 |
| Pagination | 109-119 |
| Date Published | 01/20/2010 |
| ISSN | 1096-0341 |
| Keywords | Cell Adhesion Molecules, Herpesvirus 1, Human, Viral Envelope Proteins, Virus Internalization |
| Abstract | Entry of herpes simplex virus (HSV) occurs either by fusion at the plasma membrane or by endocytosis and fusion with an endosome. Binding of glycoprotein D (gD) to a receptor such as nectin-1 is essential in both cases. We show that virion gD triggered the rapid down-regulation of nectin-1 with kinetics similar to those of virus entry. In contrast, nectin-1 was not constitutively recycled from the surface of uninfected cells. Both the nectin-1alpha and beta isoforms were internalized in response to gD despite having different cytoplasmic tails. However, deletion of the nectin-1 cytoplasmic tail slowed down-regulation of nectin-1 and internalization of virions. These data suggest that nectin-1 interaction with a cytoplasmic protein is not required for its down-regulation. Overall, this study shows that gD binding actively induces the rapid internalization of various forms of nectin-1. We suggest that HSV activates a nectin-1 internalization pathway to use for endocytic entry. |
| DOI | 10.1016/j.virol.2009.12.034 |
| PubMed ID | 20089288 |
| PubMed Central ID | PMC536050 |