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PMID: 11312345 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Requirement of interaction of nectin-1alpha/HveC with afadin for efficient cell-cell spread of herpes simplex virus type 1.

Journal of virology ·Vol. 75 ·No. 10 ·2001-05-00 ·Pages 4734-43

Sakisaka T, Taniguchi T, Nakanishi H, Takahashi K, Miyahara M, Ikeda W, Yokoyama S, Peng YF, Yamanishi K, Takai Y

Abstract

We recently found a novel cell-cell adhesion system at cadherin-based adherens junctions (AJs), consisting at least of nectin, a Ca(2+)-independent homophilic immunoglobulin-like adhesion molecule, and afadin, an actin filament-binding protein that connects nectin to the actin cytoskeleton. Nectin is associated with cadherin through afadin and alpha-catenin. The cadherin-catenin system increases the concentration of nectin at AJs in an afadin-dependent manner. Nectin constitutes a family consisting of three members: nectin-1, -2, and -3. Nectin-1 serves as an entry and cell-cell spread mediator of herpes simplex virus type 1 (HSV-1). We studied here a role of the interaction of nectin-1alpha with afadin in entry and/or cell-cell spread of HSV-1. By the use of cadherin-deficient L cells overexpressing the full length of nectin-1alpha capable of interacting with afadin and L cells overexpressing a truncated form of nectin-1alpha incapable of interacting with afadin, we found that the interaction of nectin-1alpha with afadin increased the efficiency of cell-cell spread, but not entry, of HSV-1. This interaction did not affect the binding to nectin-1alpha of glycoprotein D, a viral component mediating entry of HSV-1 into host cells. Furthermore, the cadherin-catenin system increased the efficiency of cell-cell spread of HSV-1, although it also increased the efficiency of entry of HSV-1. It is likely that efficient cell-cell spread of HSV-1 is caused by afadin-dependent concentrated localization of nectin-1alpha at cadherin-based AJs.

MeSH Terms
Amino Acid Sequence Animals Cell Adhesion Molecules/genetics,metabolism Herpesvirus 1, Human/metabolism,physiology Humans Kinesins L Cells Mice Microfilament Proteins/metabolism Molecular Sequence Data Myosins Nectins Viral Envelope Proteins/metabolism
Chemicals
AFDN protein, human Afdn protein, mouse Cell Adhesion Molecules Microfilament Proteins NECTIN1 protein, human Nectin1 protein, mouse Nectins Viral Envelope Proteins afadin glycoprotein D, Human herpesvirus 1 Myosins Kinesins
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Sakisaka T
Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Japan.
Taniguchi T
Nakanishi H
Takahashi K
Miyahara M
Ikeda W
Yokoyama S
Peng Y F
Yamanishi K
Takai Y
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.75.10.4734-4743.2001
Published
2001-05-00
Pages
4734-43
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC114228
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.75.10.4734-4743.2001 PMC Full Text View journal details
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