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-1α and β 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.
Original language | English (US) |
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Pages (from-to) | 109-119 |
Number of pages | 11 |
Journal | Virology |
Volume | 399 |
Issue number | 1 |
DOIs | |
State | Published - Mar 30 2010 |
Externally published | Yes |
Keywords
- Down-regulation
- Endocytosis
- Entry
- Glycoprotein
- HSV
- Herpes simplex virus
- Nectin-1
- Receptor
ASJC Scopus subject areas
- Virology