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

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.

journal_name

J Virol

journal_title

Journal of virology

authors

Wilson DW,Davis-Poynter N,Minson AC

doi

10.1128/JVI.68.11.6985-6993.1994

subject

Has Abstract

pub_date

1994-11-01 00:00:00

pages

6985-93

issue

11

eissn

0022-538X

issn

1098-5514

journal_volume

68

pub_type

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