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The herpes simplex virus UL20 protein functions in glycoprotein K (gK) intracellular transport and virus-induced cell fusion are independent of UL20 functions in cytoplasmic virion envelopment

机译:糖蛋白K(gK)细胞内转运和病毒诱导的细胞融合中的单纯疱疹病毒UL20蛋白功能独立于细胞质病毒体包膜中的UL20功能

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The HSV-1 UL20 protein (UL20p) and glycoprotein K (gK) are both important determinants of cytoplasmic virion morphogenesis and virus-induced cell fusion. In this manuscript, we examined the effect of UL20 mutations on the coordinate transport and Trans Golgi Network (TGN) localization of UL20p and gK, virus-induced cell fusion and infectious virus production. Deletion of 18 amino acids from the UL20p carboxyl terminus (UL20 mutant 204t) inhibited intracellular transport and cell-surface expression of both gK and UL20, resulting in accumulation of UL20p and gK in the endoplasmic reticulum (ER) in agreement with the inability of 204t to complement UL20-null virus replication and virus-induced cell fusion. In contrast, less severe carboxyl terminal deletions of either 11 or six amino acids (UL20 mutants 211t and 216t, respectively) allowed efficient UL20p and gK intracellular transport, cell-surface expression and TGN colocalization. However, while both 211t and 216t failed to complement for infectious virus production, 216t complemented for virus-induced cell fusion, but 211t did not. These results indicated that the carboxyl terminal six amino acids of UL20p were crucial for infectious virus production, but not involved in intracellular localization of UL20p/gK and concomitant virus-induced cell fusion. In the amino terminus of UL20, UL20p mutants were produced changing one or both of the Y38 and Y49 residues found within putative phosphorylation sites. UL20p tyrosine-modified mutants with both tyrosine residues changed enabled efficient intracellular transport and TGN localization of UL20p and gK, but failed to complement for either infectious virus production, or virus-induced cell fusion. These results show that UL20p functions in cytoplasmic envelopment are separable from UL20 functions in UL20p intracellular transport, cell surface expression and virus-induced cell fusion.
机译:HSV-1 UL20蛋白(UL20p)和糖蛋白K(gK)都是细胞质病毒体形态发生和病毒诱导的细胞融合的重要决定因素。在本手稿中,我们检查了UL20突变对UL20p和gK的坐标运输和反高尔基网(TGN)定位,病毒诱导的细胞融合和感染性病毒产生的影响。从UL20p羧基末端删除18个氨基酸(UL20突变体204t)会抑制gK和UL20的细胞内转运和细胞表面表达,导致UL20p和gK在内质网(ER)中积聚,这与204t的无能为力以补充UL20-null病毒复制和病毒诱导的细胞融合。相反,较不严重的11个或6个氨基酸的羧基末端缺失(分别为UL20突变体211t和216t)允许有效的UL20p和gK细胞内转运,细胞表面表达和TGN共定位。但是,尽管211t和216t均不能补充感染性病毒,但216t却可以补充病毒诱导的细胞融合,而211t则不能。这些结果表明,UL20p的羧基末端6个氨基酸对于感染性病毒的产生至关重要,但不参与UL20p / gK的细胞内定位和伴随病毒诱导的细胞融合。在UL20的氨基末端,产生了UL20p突变体,改变了假定的磷酸化位点中的Y38和Y49残基中的一个或两个。具有酪氨酸残基的UL20p酪氨酸修饰的突变体发生了改变,可实现UL20p和gK的有效细胞内转运和TGN定位,但无法补充感染性病毒的产生或病毒诱导的细胞融合。这些结果表明,UL20p在细胞质包膜中的功能与UL20在UL20p细胞内转运,细胞表面表达和病毒诱导的细胞融合中的功能是可分离的。

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