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 Citations (Scopus)

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

Fingerprint

Simplexvirus
Glycoproteins
Intercellular Junctions
nectins
Binding Sites
Ligands
Pseudopodia
Cell Adhesion Molecules
Virion
Adhesives
Actins
Epithelial Cells
Neurons

All Science Journal Classification (ASJC) codes

  • Virology

Cite this

Bhargava, Arjun K. ; Rothlauf, Paul W. ; Krummenacher, Claude. / Herpes simplex virus glycoprotein D relocates nectin-1 from intercellular contacts. In: Virology. 2016 ; Vol. 499. pp. 267-277.
@article{bb6ea1e2ff454836bff9a919b537cb44,
title = "Herpes simplex virus glycoprotein D relocates nectin-1 from intercellular contacts",
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.",
author = "Bhargava, {Arjun K.} and Rothlauf, {Paul W.} and Claude Krummenacher",
year = "2016",
month = "12",
day = "1",
doi = "10.1016/j.virol.2016.09.019",
language = "English (US)",
volume = "499",
pages = "267--277",
journal = "Virology",
issn = "0042-6822",
publisher = "Academic Press Inc.",

}

Herpes simplex virus glycoprotein D relocates nectin-1 from intercellular contacts. / Bhargava, Arjun K.; Rothlauf, Paul W.; Krummenacher, Claude.

In: Virology, Vol. 499, 01.12.2016, p. 267-277.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Herpes simplex virus glycoprotein D relocates nectin-1 from intercellular contacts

AU - Bhargava, Arjun K.

AU - Rothlauf, Paul W.

AU - Krummenacher, Claude

PY - 2016/12/1

Y1 - 2016/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84991278499&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84991278499&partnerID=8YFLogxK

U2 - 10.1016/j.virol.2016.09.019

DO - 10.1016/j.virol.2016.09.019

M3 - Article

C2 - 27723487

AN - SCOPUS:84991278499

VL - 499

SP - 267

EP - 277

JO - Virology

JF - Virology

SN - 0042-6822

ER -