Open reading frame P - A herpes simplex virus gene repressed during productive infection encodes a protein that binds a splicing factor and reduces synthesis of viral proteins made from spliced mRNA
Open reading frame P - A herpes simplex virus gene repressed during productive infection encodes a protein that binds a splicing factor and reduces synthesis of viral proteins made from spliced mRNA
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DOI：
10.1073/pnas.93.19.10423
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发表时间：
1996-09-17
影响因子：
11.1
通讯作者：
Roizman, B
中科院分区：
文献类型：
--
作者：
Bruni, R;Roizman, B
开放阅读框P（ORF P）位于潜伏感染期间转录的单纯疱疹病毒1的结构域和DNA链上。ORF P在生产性感染的细胞中不表达，这是由于主要病毒调节蛋白与其高亲和力结合位点的结合所造成的抑制。在携带去抑制基因的突变病毒感染的细胞中，ORF P蛋白被广泛地后加工。我们报告ORF P与剪接因子SF 2/ASF的组分相互作用，拉下SM抗原的组分，并与感染细胞核中的剪接因子共定位。ORF P蛋白可能具有调节病毒基因表达的作用，特别是在主要调节蛋白不表达的潜伏感染感觉神经元等情况下，这一假设得到了以下证据的支持：在感染突变体的细胞中，ORF P基因被去抑制，调节基因α 0和α 22的产物在感染早期数量减少，但在感染后期恢复。由这些基因编码的蛋白质由剪接的mRNA制成，并且这些蛋白质在感染后期的恢复程度与ORF P蛋白的后加工形式的积累程度相关。
The open reading frame P (ORF P) is located in the domain and on the DNA strand of the herpes simplex virus 1 transcribed during latent infection. ORF P is not expressed in productively infected cells as a consequence of repression by the binding of the major viral regulatory protein to its high-affinity binding site, In cells infected with a mutant virus carrying a derepressed gene, ORF P protein is extensively posttranslationally processed, We report that ORF P interacts with a component of the splicing factor SF2/ASF, pulls down a component of the SM antigens, and colocalizes with splicing factors in nuclei of infected cells. The hypothesis that ORF P protein may act to regulate viral gene expression, particularly in situations such as latently infected sensory neurons in which the major regulatory protein is not expressed, is supported by the evidence that in cells infected with a mutant in which the ORF P gene was derepressed, the products of the regulatory genes alpha 0 and alpha 22 are reduced in amounts early in infection but recover late in infection. The proteins encoded by these genes are made from spliced mRNAs, and the extent of recovery of these proteins Late in infection correlates with the extent of accumulation of posttranslationally processed forms of ORF P protein.