Aj. Stevenson et al., PROCESSING AND INTRACELLULAR-LOCALIZATION OF THE HERPES-SIMPLEX VIRUSTYPE-1 PROTEINASE, Journal of General Virology, 78, 1997, pp. 671-675
The herpes simplex virus type 1 (HSV-1) capsid protein VP24 (encoded b
y UL26) was expressed as a GST-fusion protein and used to prepare a gr
oup of monoclonal antibodies. These were used to characterize the prot
ein in capsids and virus infected cells and demonstrated that it exist
s as two polypeptide species. The nature of the relationship between t
hese two species was investigated and found to be associated with disu
lphide bonding. Under non-reducing conditions a species corresponding
to dimers of VP24 was identified in preparations of B capsids, the sit
e of action of the proteinase. Biochemical subcellular fractionation s
tudies suggested that only cleaved forms of UL26 and UL26.5 gene produ
cts could be detected in the nucleus of the infected cell at early tim
es postinfection.