title: 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.
authors.affiliation: Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
authors.forename: D W
authors.initials: DW
authors.lastname: Wilson
authors.forename: N
authors.initials: N
authors.lastname: Davis-Poynter
authors.forename: A C
authors.initials: AC
authors.lastname: Minson
mesh_terms: D000409:Alanine; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002522:Chlorocebus aethiops; D005816:Genetic Complementation Test; D018259:Herpesvirus 1, Human / Q000502:physiology*; D008969:Molecular Sequence Data; D009154:Mutation; D013329:Structure-Activity Relationship; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*
chemical_list: D014759:Viral Envelope Proteins; C044200:glycoprotein H, herpes simplex virus type 1; D000409:Alanine