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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.

SUBMITTER: Zhou W 

PROVIDER: S-EPMC3911704 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

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Mutations in the amino terminus of herpes simplex virus type 1 gL can reduce cell-cell fusion without affecting gH/gL trafficking.

Zhou Wenbo W   Chen Feng F   Klyachkin Yuri Y   Sham Yuk Y YY   Geraghty Robert J RJ  

Journal of virology 20131023 1


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. ...[more]

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