Glycoprotein K specified by herpes simplex virus type 1 is expressed on virions as a Golgi complex-dependent glycosylated species and functions in virion entry.
To facilitate detection of glycoprotein K (gK) specified by herpes simplex virus, a 12-amino-acid epitope tag was inserted within gK domain III. Recombinant virus gKprotC-DIII, expressing the tagged gK, was isolated. This virus formed wild-type plaques and replicated as efficiently as the wild-type KOS virus in Vero cells. Anti-protein C MAb detected high-mannose and Golgi complex-dependent glycosylated gK within cells as well as on purified virions. The gK-null virus DeltagK (gK(-/-)) entered Vero cells substantially more slowly than the wild-type KOS (gK(+/+)), while DeltagK virus grown in complementing VK302 cells (gK(-/+)) entered with entry kinetics similar to those of the KOS virus.
Foster
T P
TP
Department of Pathobiological Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, Louisiana 70803, USA.
Rybachuk
G V
GV
Kousoulas
K G
KG
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002522:Chlorocebus aethiops; D006031:Glycosylation; D006056:Golgi Apparatus / Q000378:metabolism*; D008969:Molecular Sequence Data; D018139:Simplexvirus / Q000737:chemistry / Q000502:physiology*; D014709:Vero Cells; D014764:Viral Proteins / Q000502:physiology*; D014771:Virion / Q000737:chemistry / Q000502:physiology*
D000911:Antibodies, Monoclonal; C072448:UL53 protein, Human herpesvirus 1; D014764:Viral Proteins