Fusion activity of lipid-anchored envelope glycoproteins of herpes simplex virus type 1

Natasha A. Jones, Robert J. Geraghty

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


Expression of the herpes simplex virus type 1 (HSV-1) glycoproteins gB, gD, gH, and gL is necessary and sufficient to cause cell fusion. To identify the requirements for a membrane-spanning domain in HSV-1 glycoprotein-induced cell fusion, we created gB, gD, and gH mutants with transmembrane and cytoplasmic domains replaced by a glycosylphosphatidylinositol (gpi)-addition sequence. The corresponding gBgpi, gDgpi, and gHgpi proteins were expressed with wild-type efficiency at the cell surface and were linked to the plasma membrane via a gpi anchor. The gDgpi mutant promoted cell fusion near wild-type gD levels when co-expressed with gB, gH, and gL in a cell-mixing fusion assay, indicating that the gD transmembrane and cytoplasmic domains were not required for fusion activity. A plasma membrane link was required for fusion because a gD mutant lacking a transmembrane and cytoplasmic domain was nonfunctional for fusion. The gDgpi mutant was also able to cooperate with wild-type gB, gH, and gL to form syncytia, albeit at a size smaller than those formed in the wild-type situation. The gBgpi and gHgpi mutants were unable to promote fusion when expressed with the other wild-type viral glycoproteins, highlighting the requirement of the specific transmembrane and cytoplasmic domains for gB and gH function.

Original languageEnglish (US)
Pages (from-to)213-228
Number of pages16
Issue number1
StatePublished - Jun 20 2004
Externally publishedYes

Bibliographical note

Funding Information:
This investigation was funded by an American Cancer Society Institutional Research Grant #85-001-13-IRG and a National Institutes of Health Grant #AI51476.


  • Fusion
  • Glycosylphosphatidylinositol
  • Herpes simplex virus
  • Nectin-1
  • Phosphatidylinositol phospholipase C
  • Syncytium
  • Transmembrane domain
  • gB
  • gD
  • gH


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