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首页> 美国卫生研究院文献>Journal of Virology >Posttranslational Processing of Infected Cell Protein 22 Mediated by Viral Protein Kinases Is Sensitive to Amino Acid Substitutions at Distant Sites and Can Be Cell-Type Specific
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Posttranslational Processing of Infected Cell Protein 22 Mediated by Viral Protein Kinases Is Sensitive to Amino Acid Substitutions at Distant Sites and Can Be Cell-Type Specific

机译：由病毒蛋白激酶介导的感染细胞蛋白22的翻译后加工对远端位点的氨基酸取代敏感，并且可能是细胞类型特异性的

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Infected cell protein 22 (ICP22) is posttranslationally phosphorylated by the viral kinases encoded by US3 and UL13 and nucleotidylylated by casein kinase II. In rabbit and rodent cells and in primary human fibroblasts infected with mutants from which the α22 gene encoding ICP22 had been deleted, a subset of late (γ2) gene products exemplified by UL38 and US11 proteins are expressed at a reduced level, as measured by the accumulation of both mRNA and protein. The same phenotype was observed in cells infected with mutants lacking the UL13 gene. The focus of this report is on three serine- and threonine-rich domains of ICP22. Two of these domains are homologs located between residues 38 to 66 and 300 to 328. The third domain is near the carboxyl terminus and contains the sequence T374SS. The results were as follows. (i) Alanine substitutions in the amino-terminal homolog precluded the posttranslational processing of ICP22 in rabbit skin cells and in Vero cells but had no effect on the accumulation of either US11 or UL38 protein. (ii) Alanine substitutions in the carboxyl-terminal homolog had no effect on posttranslational processing of ICP22 accumulating in Vero cells but precluded full processing of ICP22 accumulating in rabbit skin cells. The effect on accumulation of UL38 and US11 proteins was insignificant in Vero cells and minimal in rabbit skin cells. (iii) Substitutions of alanine for the threonine and serines in the third domain precluded full processing of ICP22 and caused a reduction of accumulation of US11 and UL38 proteins. These results indicate the following. (i) The posttranslational processing of ICP22 is sensitive to mutations within the domains of ICP22 tested and is cell-type dependent. (ii) Posttranslational processing of ICP22 is not required for accumulation of UL38 and US11 proteins to the same level as that seen in cells infected with the wild-type virus. (iii) The T374SS sequence shared by ICP22 and the US1.5 proteins is essential for the accumulation of a subset of γ2 proteins exemplified by US11 and UL38 and is the first step in mapping of the sequences necessary for optimal accumulation of US11 and UL38 proteins.
机译：感染的细胞蛋白22（ICP22）被US3和UL13编码的病毒激酶翻译后磷酸化，并被酪蛋白激酶II核苷酸化。在兔和啮齿动物细胞中以及感染了突变体的原代人成纤维细胞中，已删除了编码ICP22的α22基因，通过UL38和US11蛋白举例说明的晚期（γ2）基因产物的子集以降低的水平表达。 mRNA和蛋白质的积累。在感染缺少UL13基因的突变体的细胞中观察到相同的表型。本报告的重点是ICP22的三个富含丝氨酸和苏氨酸的域。这些结构域中的两个是位于残基38至66和300至328之间的同源物。第三个结构域位于羧基末端附近，并包含序列T374SS。结果如下。 （i）氨基末端同源物中的丙氨酸取代排除了ICP22在兔皮细胞和Vero细胞中的翻译后加工，但对US11或UL38蛋白的积累没有影响。 （ii）在羧基末端同源物中的丙氨酸取代对在Vero细胞中积累的ICP22的翻译后加工没有影响，但是排除了在兔皮肤细胞中积累的ICP22的全部加工。对UL38和US11蛋白积累的影响在Vero细胞中微不足道，而在兔皮肤细胞中微不足道。 （iii）在第三个域中用丙氨酸替代苏氨酸和丝氨酸妨碍了ICP22的全面处理，并导致US11和UL38蛋白的积累减少。这些结果表明如下。 （i）ICP22的翻译后加工过程对所测试的ICP22域内的突变敏感，并且取决于细胞类型。 （ii）UL38和US11蛋白的积累达到与野生型病毒感染的细胞相同的水平，不需要ICP22的翻译后处理。 （iii）ICP22和US1.5蛋白质共有的T374SS序列对于γ2蛋白质子集的积累至关重要，例如U S 11和U L 38和是定位U S 11和U L 38蛋白最佳积累所必需的序列的第一步。

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