title: Mutations in the amino terminus of herpes simplex virus type 1 gL can reduce cell-cell fusion without affecting gH/gL trafficking.
abstract: The gH/gL heterodimer represents two of the four herpes simplex virus glycoproteins necessary and sufficient for membrane fusion. We generated deletions and point mutations covering gL residues 24 to 43 to investigate that region's role in gH/gL intracellular trafficking and in membrane fusion. Multiple mutants displayed a 40 to 60% reduction in cell fusion with no effect on gH/gL trafficking. The amino terminus of gL plays an important role in the gH/gL contribution to membrane fusion.
authors.affiliation: Center for Drug Design, University of Minnesota, Minneapolis, Minnesota, USA.
authors.forename: Wenbo
authors.initials: W
authors.lastname: Zhou
authors.forename: Feng
authors.initials: F
authors.lastname: Chen
authors.forename: Yuri
authors.initials: Y
authors.lastname: Klyachkin
authors.forename: Yuk Y
authors.initials: YY
authors.lastname: Sham
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Geraghty
mesh_terms: D000595:Amino Acid Sequence; D002459:Cell Fusion; D018259:Herpesvirus 1, Human / Q000502:physiology*; D008969:Molecular Sequence Data; D009154:Mutation; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*
chemical_list: D014764:Viral Proteins