The nectin-1alpha transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins.
The nectin-1alpha transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins.
复制标题
Nectin-1α 跨膜结构域（而非胞质尾部）影响 HSV-1 糖蛋白诱导的细胞融合。
DOI：
10.1016/j.virol.2005.05.031
复制
发表时间：
2005
期刊：
影响因子：
3.7
通讯作者：
Geraghty,RobertJ
中科院分区：
文献类型：
--
作者：
Subramanian,RaviP;Dunn,JenniferE;Geraghty,RobertJ
Nectin-1是单纯疱疹病毒（HSV）的受体，免疫球蛋白超家族的成员，和细胞粘附分子。为了研究nectin-1α参与细胞融合的结构域，我们测量了nectin-1α/nectin-2α嵌合体、nectin-1α/CD 4嵌合体以及nectin-1α的跨膜结构域和胞质尾突变体促进HSV-1糖蛋白诱导的细胞融合的能力。我们的研究结果表明，只有嵌合体和突变体包含整个V样结构域和连接到质膜赋予细胞融合活性。nectin-1的跨膜结构域和胞质尾区对于测试的任何病毒受体或细胞粘附功能都不是必需的。因此，与nectin-1α胞质尾区结合的细胞胞质因子不影响病毒进入或细胞融合。有趣的是，当nectin-1α和gD的跨膜结构域被糖基磷脂酰肌醇栓链取代时，细胞融合的效率降低，表明跨膜结构域可能在融合中的gD/nectin-1α相互作用中起调节作用。
Nectin-1 is a receptor for herpes simplex virus (HSV), a member of the immunoglobulin superfamily, and a cellular adhesion molecule. To study domains of nectin-1α involved in cell fusion, we measured the ability of nectin-1α/nectin-2α chimeras, nectin-1α/CD4 chimeras, and transmembrane domain and cytoplasmic tail mutants of nectin-1α to promote cell fusion induced by HSV-1 glycoproteins. Our results demonstrate that only chimeras and mutants containing the entire V-like domain and a link to the plasma membrane conferred cell-fusion activity. The transmembrane domain and cytoplasmic tail of nectin-1 were not required for any viral receptor or cell adhesion function tested. Cellular cytoplasmic factors that bind to the nectin-1α cytoplasmic tail, therefore, did not influence virus entry or cell fusion. Interestingly, the efficiency of cell fusion was reduced when membrane-spanning domains of nectin-1α and gD were replaced by glycosylphosphatidylinositol tethers, indicating that transmembrane domains may play a modulatory role in the gD/nectin-1α interaction in fusion.