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Requirement of Interaction of Nectin-1α/HveC with Afadin for Efficient Cell-Cell Spread of Herpes Simplex Virus Type 1

By Toshiaki Sakisaka, Tomokuni Taniguchi, Hiroyuki Nakanishi, Kenichi Takahashi, Masako Miyahara, Wataru Ikeda, Shigekazu Yokoyama, Ying-Feng Peng, Koichi Yamanishi and Yoshimi Takai


We recently found a novel cell-cell adhesion system at cadherin-based adherens junctions (AJs), consisting at least of nectin, a Ca2+-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 α-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-1α 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-1α capable of interacting with afadin and L cells overexpressing a truncated form of nectin-1α incapable of interacting with afadin, we found that the interaction of nectin-1α with afadin increased the efficiency of cell-cell spread, but not entry, of HSV-1. This interaction did not affect the binding to nectin-1α 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-1α at cadherin-based AJs

Topics: Virus-Cell Interactions
Publisher: American Society for Microbiology
Year: 2001
DOI identifier: 10.1128/JVI.75.10.4734-4743.2001
OAI identifier:
Provided by: PubMed Central
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