Herpes simplex virus glycoprotein D relocates nectin-1 from intercellular contacts

Arjun K. Bhargava, Paul W. Rothlauf, Claude Krummenacher

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Herpes simplex virus (HSV) uses the cell adhesion molecule nectin-1 as a receptor to enter neurons and epithelial cells. The viral glycoprotein D (gD) is used as a non-canonical ligand for nectin-1. The gD binding site on nectin-1 overlaps with a functional adhesive site involved in nectin-nectin homophilic trans-interaction. Consequently, when nectin-1 is engaged with a cellular ligand at cell junctions, the gD binding site is occupied. Here we report that HSV gD is able to disrupt intercellular homophilic trans-interaction of nectin-1 and induce a rapid redistribution of nectin-1 from cell junctions. This movement does not require the receptor's interaction with the actin-binding adaptor afadin. Interaction of nectin-1 with afadin is also dispensable for virion surfing along nectin-1-rich filopodia. Cells seeded on gD-coated surfaces also fail to accumulate nectin-1 at cell contact. These data indicate that HSV gD affects nectin-1 locally through direct interaction and more globally through signaling.

Original languageEnglish (US)
Pages (from-to)267-277
Number of pages11
JournalVirology
Volume499
DOIs
StatePublished - Dec 1 2016

All Science Journal Classification (ASJC) codes

  • Virology

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