Sariyer Ilker K, Akan Ilhan, Palermo Victoria, Gordon Jennifer, Khalili Kamel, Safak Mahmut
Department of Neuroscience, Center for Neurovirology, Laboratory of Molecular Neurovirology, Temple University School of Medicine, 1900 North 12th St., 015-96, Rm. 442, Philadelphia, Pennsylvania 19122, USA.
J Virol. 2006 Apr;80(8):3893-903. doi: 10.1128/JVI.80.8.3893-3903.2006.
Many eukaryotic and viral regulatory proteins are known to undergo posttranslational modifications including phosphorylation, which plays a critical role in many aspects of cell function. Previous studies from our and other laboratories indicated that the JC virus (JCV) late regulatory protein, agnoprotein, plays an important role in the JCV life cycle. Agnoprotein contains several potential phosphorylation sites, including Ser7, Ser11, and Thr21, which are potential targets for the serine/threonine-specific protein kinase C (PKC). In this study, we investigated the functional significance of these phosphorylation sites for the activity of agnoprotein. In vitro and in vivo kinase assays demonstrated that agnoprotein is a target for phosphorylation by PKC. In addition, each of the PKC phosphorylation sites was mutated to Ala singly and in combination, and the effects of these mutations on the JCV life cycle were analyzed. Although the expression of each mutant agnoprotein was detectable during the infection cycle, virus containing each of these mutations failed to propagate. These results contrast with those obtained with an agnoprotein start codon point (Pt) mutant where agnoprotein expression was completely inhibited. The Pt mutant was viable but replicates less efficiently than the wild type (WT). Moreover, conservative substitutions at PKC phosphorylation sites (Ser7, Ser11, and Thr21 to Asp) resulted in a viable virus, which further demonstrate the importance of these sites on agnoprotein function. Further analysis of the mutants by viral release assay and electron microscopy studies revealed that viral particles were efficiently released from infected cells and morphologically indistinguishable from those of WT but were deficient in DNA content. This may account for the defective propagation of the mutants. These results imply that phosphorylated forms of agnoprotein may have essential functions in the viral life cycle and serve as potential targets for therapeutic interventions to limit JCV propagation and JCV-induced diseases.
已知许多真核生物和病毒调节蛋白会经历翻译后修饰,包括磷酸化,这在细胞功能的许多方面都起着关键作用。我们实验室和其他实验室先前的研究表明,JC病毒(JCV)晚期调节蛋白agnoprotein在JCV生命周期中起重要作用。Agnoprotein包含几个潜在的磷酸化位点,包括Ser7、Ser11和Thr21,它们是丝氨酸/苏氨酸特异性蛋白激酶C(PKC)的潜在作用靶点。在本研究中,我们研究了这些磷酸化位点对agnoprotein活性的功能意义。体外和体内激酶分析表明,agnoprotein是PKC磷酸化的作用靶点。此外,将每个PKC磷酸化位点单独或组合突变为丙氨酸,并分析这些突变对JCV生命周期的影响。尽管在感染周期中可检测到每个突变型agnoprotein的表达,但含有这些突变的病毒均无法增殖。这些结果与agnoprotein起始密码子点(Pt)突变体的结果形成对比,在该突变体中agnoprotein的表达被完全抑制。Pt突变体是有活力的,但复制效率低于野生型(WT)。此外,PKC磷酸化位点的保守替换(Ser7、Ser11和Thr21替换为Asp)产生了一种有活力的病毒,这进一步证明了这些位点对agnoprotein功能的重要性。通过病毒释放分析和电子显微镜研究对突变体进行的进一步分析表明,病毒颗粒能从感染细胞中有效释放,并且在形态上与WT病毒颗粒无法区分,但DNA含量不足。这可能解释了突变体繁殖缺陷的原因。这些结果表明,磷酸化形式的agnoprotein可能在病毒生命周期中具有重要功能,并可作为限制JCV增殖和JCV诱导疾病的治疗干预的潜在靶点。