D. Simonin et al., PHOSPHORYLATION OF HERPES-SIMPLEX VIRUS TYPE-1 US11 PROTEIN IS INDEPENDENT OF VIRAL GENOME EXPRESSION, Electrophoresis, 16(7), 1995, pp. 1317-1322
The Us11 protein is a true late gene product of herpes simplex virus t
ype 1 (HSV-1), whose exact function is unknown but which exhibits RNA-
binding properties and which is phosphorylated on serine residues. In
order to determine whether the Us11 protein is phosphorylated by cellu
lar kinase(s) or by virally encoded kinase(s), the Us11 gene has been
cloned and transiently expressed in HeLa cells. In addition, HeLa-deri
ved cell lines have been selected for their ability to express Us11 pr
otein constitutively. P-32-Labeling and analysis by two-dimensional el
ectrophoresis of transiently and constitutively expressed Us11 protein
demonstrated that, indeed, multiple phosphorylation of the protein oc
curs in absence of HSV-1 genome expression, indicating that the protei
n behaves as a natural substrate for cellular kinase(s). In addition,
a sequence heterogeneity of the Us11 protein, due to a difference in t
he number of SPREPR repeats, has been characterized between different
strains of HSV-1.