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 journalArticle

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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