Properties of the novel herpes simplex virus type 1 origin binding protein, OBPC.
We have recently identified a novel 53-kDa herpes simplex virus type 1 (HSV-1) protein encoded by, and in frame with, the 3' half of the UL9 open reading frame, designated OBPC (K. Baradaran, C. Dabrowski and P. A. Schaffer, J. Virol. 68:4251-4261, 1994). Here we show that OBPC is a nuclear protein synthesized at both early and late times postinfection. In gel-shift assays in vitro-synthesized OBPC bound to oriS site I DNA to form a complex identical in mobility to complex A, generated with infected cell extracts and site I DNA. OBPC inhibited both plaque formation and viral DNA replication in transient assays, consistent with its ability to bind to site I DNA and its limited ability to interact with other essential DNA replication proteins. These properties suggest that OBPC may play a role in the initiation, elongation, or packaging of viral DNA.
Baradaran
K
K
Committee on Virology and Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
Hardwicke
M A
MA
Dabrowski
C E
CE
Schaffer
P A
PA
D004268:DNA-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D018139:Simplexvirus / Q000378:metabolism*; D014764:Viral Proteins / Q000302:isolation & purification* / Q000378:metabolism
D004268:DNA-Binding Proteins; D014764:Viral Proteins; C064565:UL9 protein, Human herpesvirus 1