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. 1996 Aug;70(8):5673–5679. doi: 10.1128/jvi.70.8.5673-5679.1996

Properties of the novel herpes simplex virus type 1 origin binding protein, OBPC.

K Baradaran 1, M A Hardwicke 1, C E Dabrowski 1, P A Schaffer 1
PMCID: PMC190533  PMID: 8764087

Abstract

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.

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Selected References

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