新型单纯疱疹病毒1型起始结合蛋白OBPC的特性
Properties of the novel herpes simplex virus type 1 origin binding protein, OBPC.
作者信息
Baradaran K, Hardwicke M A, Dabrowski C E, Schaffer P A
机构信息
Committee on Virology and Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
出版信息
J Virol. 1996 Aug;70(8):5673-9. doi: 10.1128/JVI.70.8.5673-5679.1996.
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.
摘要
我们最近鉴定出一种由单纯疱疹病毒1型（HSV-1）UL9开放阅读框3'端编码且读码框正确的新型53 kDa蛋白，命名为OBPC（K. Baradaran、C. Dabrowski和P. A. Schaffer，《病毒学杂志》68:4251-4261，1994年）。在此我们表明，OBPC是一种在感染后早期和晚期均能合成的核蛋白。在凝胶迁移实验中，体外合成的OBPC与oriS位点I的DNA结合，形成一种迁移率与用感染细胞提取物和位点I DNA产生的复合物A相同的复合物。在瞬时实验中，OBPC抑制噬斑形成和病毒DNA复制，这与其结合位点I DNA的能力以及与其他必需的DNA复制蛋白相互作用的有限能力一致。这些特性表明，OBPC可能在病毒DNA的起始、延伸或包装过程中发挥作用。
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