THE UL13 VIRION PROTEIN OF HERPES-SIMPLEX VIRUS TYPE-1 IS PHOSPHORYLATED BY A NOVEL VIRUS-INDUCED PROTEIN-KINASE
THE UL13 VIRION PROTEIN OF HERPES-SIMPLEX VIRUS TYPE-1 IS PHOSPHORYLATED BY A NOVEL VIRUS-INDUCED PROTEIN-KINASE
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DOI：
10.1099/0022-1317-73-2-303
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发表时间：
1992-02-01
影响因子：
3.8
通讯作者：
ORR, AC
中科院分区：
文献类型：
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作者：
CUNNINGHAM, C;DAVISON, AJ;ORR, AC
单纯疱疹病毒1型（HSV-1）诱导感染细胞核中的蛋白激酶（PK）活性。在体外，该酶能够磷酸化外源性酪蛋白（尽管效率低下），但不能磷酸化鱼精蛋白，可以使用ATP或β-GTP作为磷酸供体，受高盐浓度刺激，对肝素的抑制不敏感。基于这些特性，PK似乎不同于先前描述的细胞酶和由病毒US 3基因编码的细胞质PK。该酶在体外的主要底物是M（r）为57000（Vmw 57）的病毒诱导蛋白。使用HSV-1和HSV-2之间的重组体将编码Vmw 57的基因定位到含有基因UL 9至UL 15的病毒基因组区域。单特异性兔抗血清的使用表明，Vmw 57是由基因UL 13编码的病毒体结构蛋白。这些结果，结合以前的报告，UL 13蛋白含有PK序列基序，支持的概念，即核PK和Vmw 57是相同的，观察到的反应性是由于自磷酸化。
Herpes simplex virus type 1 (HSV-1) induces a protein kinase (PK) activity in infected cell nuclei. In vitro, the enzyme is able to phosphorylate exogenous casein (albeit inefficiently) but not protamine, can use ATP or (GTP as a phosphate donor, is stimulated by high salt concentrations and is insensitive to inhibition by heparin. On the basis of these properties, the PK appears to be distinct from previously described cellular enzymes and from the cytoplasmic PK encoded by the viral US3 gene. A major substrate of the enzyme in vitro is a virus-induced protein with an M(r) of 57000 (Vmw57). The gene encoding Vmw57 was mapped using recombinants between HSV-1 and HSV-2 to a region of the virus genome containing genes UL9 to UL15. Use of a monospecific rabbit antiserum showed that Vmw57 is a virion structural protein encoded by gene UL13. These results, in conjunction with previous reports that the UL13 protein contains PK sequence motifs, support the notions that the nuclear PK and Vmw57 are identical, and that the observed reactivity is due to autophosphorylation.