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The nectin-1alpha transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins.

Abstract：

: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-1alpha involved in cell fusion, we measured the ability of nectin-1alpha/nectin-2alpha chimeras, nectin-1alpha/CD4 chimeras, and transmembrane domain and cytoplasmic tail mutants of nectin-1alpha 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-1alpha 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-1alpha and gD were replaced by glycosylphosphatidylinositol tethers, indicating that transmembrane domains may play a modulatory role in the gD/nectin-1alpha interaction in fusion.

journal_name

Virology

journal_title

Virology

authors

Subramanian RP,Dunn JE,Geraghty RJ

doi

10.1016/j.virol.2005.05.031

subject

Has Abstract

pub_date

2005-09-01 00:00:00

pages

176-91

issue

2

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(05)00331-4

journal_volume

339

pub_type

杂志文章

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