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

Ravi P. Subramanian, Jennifer E. Dunn, Robert J. Geraghty

Research output: Contribution to journalArticle

12 Scopus citations

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-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.

Original languageEnglish (US)
Pages (from-to)176-191
Number of pages16
JournalVirology
Volume339
Issue number2
DOIs
StatePublished - Sep 1 2005
Externally publishedYes

Keywords

  • Cytoplasmic tail
  • Fusion
  • Glycosylphosphatidylinositol
  • Herpes simplex
  • Nectin-1
  • Syncytium
  • Transmembrane domain

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