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Journal of Virology, May 2001, p. 4734-4743, Vol. 75, No. 10
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.10.4734-4743.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Requirement of Interaction of Nectin-1
/HveC with
Afadin for Efficient Cell-Cell Spread of Herpes Simplex Virus
Type 1
Toshiaki
Sakisaka,1,2,
Tomokuni
Taniguchi,3
Hiroyuki
Nakanishi,1,2
Kenichi
Takahashi,2,
Masako
Miyahara,2
Wataru
Ikeda,1
Shigekazu
Yokoyama,1
Ying-Feng
Peng,1
Koichi
Yamanishi,3 and
Yoshimi
Takai1,2,*
Department of Molecular Biology and
Biochemistry1 and Department of
Microbiology,3 Osaka University Graduate School
of Medicine/Faculty of Medicine, Suita 565-0871, and The
Takai Biotimer Project,§ ERATO, Japan Science and
Technology Corporation, c/o JCR Pharmaceuticals Co., Ltd., Nishi-ku,
Kobe 651-2241,2 Japan
Received 14 August 2000/Accepted 23 February 2001
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
-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-1
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-1
capable of interacting with afadin and L
cells overexpressing a truncated form of nectin-1
incapable of
interacting with afadin, we found that the interaction of nectin-1
with afadin increased the efficiency of cell-cell spread, but not
entry, of HSV-1. This interaction did not affect the binding to
nectin-1
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-1
at cadherin-based AJs.
*
Corresponding author. Mailing address: Department of
Molecular Biology and Biochemistry, Osaka University Graduate School of
Medicine/Faculty of Medicine, Suita 565-0871, Japan. Phone: 81-6-6879-3410. Fax: 81-6-6879-3419. E-mail:
ytakai{at}molbio.med.osaka-u.ac.jp.

Present address: Department of Cell Biology, The Scripps Research
Institute, La Jolla, CA
92037.

Present address: JCR Pharmaceuticals Co., Ltd., Nishi-ku,
Kobe 651-2241,
Japan.
§
The Takai Biotimer Project was closed in September
1999.
Journal of Virology, May 2001, p. 4734-4743, Vol. 75, No. 10
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.10.4734-4743.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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