Requirement of interaction of nectin-1α/HveC with afadin for efficient cell-cell spread of herpes simplex virus type 1
Requirement of interaction of nectin-1α/HveC with afadin for efficient cell-cell spread of herpes simplex virus type 1
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DOI：
10.1128/jvi.75.10.4734-4743.2001
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发表时间：
2001-05-01
影响因子：
5.4
通讯作者：
Takai, Y
中科院分区：
文献类型：
--
作者：
Sakisaka, T;Taniguchi, T;Takai, Y
我们最近发现了一种新的细胞-细胞黏附系统，在钙粘蛋白为基础的黏附连接（AJs）上，至少由连接蛋白（一种Ca2+独立的血亲免疫球蛋白样黏附分子）和afadin（一种连接连接蛋白和肌动蛋白细胞骨架的肌动蛋白丝结合蛋白）组成。连接蛋白通过afadin和-catenin与钙粘蛋白相关联。钙粘蛋白-连环蛋白系统以依赖性的方式增加AJs的连接蛋白浓度。Nectin构成了一个由三个成员组成的家族：Nectin -1、-2和-3。连接蛋白-1作为1型单纯疱疹病毒（HSV-1）的进入和细胞-细胞传播介质。我们在这里研究了连接素-1 α与afadin相互作用在HSV-1进入和/或细胞-细胞传播中的作用。通过使用钙粘蛋白缺失的L细胞过表达能够与afadin相互作用的完整长度的nectin-1 α和过表达不能与afadin相互作用的截断形式的L细胞，我们发现nectin-1 α与afadin的相互作用增加了HSV-1的细胞-细胞传播效率，但没有进入细胞。这种相互作用不影响糖蛋白D与连接素-1 α的结合，糖蛋白D是一种介导HSV-1进入宿主细胞的病毒成分。此外，cadherin-catenin系统增加了HSV-1的细胞-细胞传播效率，尽管它也增加了HSV-1的进入效率。HSV-1的高效细胞-细胞传播很可能是由依赖于钙粘蛋白的连接素-1 α的集中定位引起的。
We recently found a novel cell-cell adhesion system at cadherin-based adherens junctions (AJs), consisting at least of nectin, a Ca2+-independent hemophilic 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-1 alpha 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 alpha, capable of interacting with afadin and L cells overexpressing a truncated form of nectin-1 alpha incapable of interacting with afadin, we found that the interaction of nectin-1 alpha 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 alpha 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 alpha at cadherin-based AJs.