Glycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entry

Katie M. Stiles, Claude Krummenacher

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

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 languageEnglish (US)
Pages (from-to)109-119
Number of pages11
JournalVirology
Volume399
Issue number1
DOIs
StatePublished - Mar 30 2010

Keywords

  • Down-regulation
  • Endocytosis
  • Entry
  • Glycoprotein
  • HSV
  • Herpes simplex virus
  • Nectin-1
  • Receptor

ASJC Scopus subject areas

  • Virology

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