人类免疫缺陷病毒1型Vpr的磷酸化调节细胞周期停滞。
Phosphorylation of human immunodeficiency virus type 1 Vpr regulates cell cycle arrest.
作者信息
Zhou Y, Ratner L
机构信息
Departments of Medicine, Pathology, and Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
出版信息
J Virol. 2000 Jul;74(14):6520-7. doi: 10.1128/jvi.74.14.6520-6527.2000.
Abstract
Human immunodeficiency virus type 1 (HIV-1) Vpr regulates nuclear transport of the viral preintegration complex, G(2) cell cycle arrest, and transcriptional transactivation. We asked whether phosphorylation could affect Vpr activity. Vpr was found to be phosphorylated on serine residues in transiently transfected and infected cells. Residues 79, 94, and 96 were all found to be phosphorylated, as assessed by alanine mutations. Mutation of Ser-79 to Ala abrogated effects of Vpr on cell cycle progression, whereas mutation of Ser-94 and Ser-96 had no effect. Simultaneous mutation of all three Vpr serine residues attenuated HIV-1 replication in macrophages, whereas single and double Ser mutations had no effect.
摘要
1型人类免疫缺陷病毒（HIV-1）的Vpr蛋白可调控病毒前整合复合物的核转运、G2期细胞周期阻滞以及转录反式激活。我们探究了磷酸化是否会影响Vpr的活性。在瞬时转染和感染的细胞中，Vpr蛋白在丝氨酸残基上发生了磷酸化。通过丙氨酸突变分析发现，第79、94和96位残基均发生了磷酸化。将Ser-79突变为Ala可消除Vpr对细胞周期进程的影响，而Ser-94和Ser-96的突变则没有影响。Vpr蛋白所有三个丝氨酸残基同时发生突变会减弱HIV-1在巨噬细胞中的复制，而单个和两个丝氨酸残基的突变则没有影响。
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