Mutations in the cytoplasmic tail of herpes simplex virus glycoprotein H suppress cell fusion by a syncytial strain

Duncan W. Wilson, Nick Davis-Poynter, Anthony C. Minson

Research output: Contribution to journalArticle

65 Scopus citations

Abstract

We have developed a complementation assay, using transiently transfected COS cells, to facilitate a molecular analysis of the herpes simplex virus type 1 glycoprotein gH. When infected by a gH-null syncytial virus, COS cells expressing wild-type gH generate infectious progeny virions and form a syncytium with neighboring cells. By deletion and point mutagenesis, we have found particular residues in the gH cytoplasmic tail to be essential for generation of a syncytium but apparently dispensable for production of infectious virions. This study emphasizes the different requirements for cell-cell and cell-envelope fusion and demonstrates that changes in the non- syn locus UL22-gH can reverse the syncytial phenotype.

Original languageEnglish (US)
Pages (from-to)6985-6993
Number of pages9
JournalJournal of virology
Volume68
Issue number11
StatePublished - Nov 1 1994

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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