Post-translational modification of the tegument proteins (VP13 and VP14) of herpes simplex virus type 1 by glycosylation and phosphorylation.
VP13 and VP14, major tegument proteins of herpes simplex virus type 1 (HSV-1) and the products of the UL47 gene, have been shown by partial proteolytic mapping to have closely related protein sequences. These proteins are phosphorylated in virus-infected cells, but not in preparations of purified virus. They also contain O-linked oligosaccharide units which include beta-1,4-N-acetyl galactosamine residues, as demonstrated by the binding of Dolichos biflorus lectin. This modification was detected only in purified virus and appears to be restricted to VP13/14 and VP22, another HSV-1 tegument protein.
Meredith
D M
DM
Department of Microbiology, University of Leeds, U.K.
Lindsay
J A
JA
Halliburton
I W
IW
Whittaker
G R
GR
D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D018139:Simplexvirus / Q000378:metabolism*; D014763:Viral Matrix Proteins / Q000378:metabolism*
D014763:Viral Matrix Proteins