Molecular anatomy of the subcellular localization and nuclear import mechanism of herpes simplex virus 1 UL6

被引：9

作者：

Cai, Mingsheng ^{[1
]}

Ou, Xiaowen ^{[1
]}

Li, Yiwen ^{[1
]}

Zou, Xingmei ^{[1
]}

Xu, Zuo ^{[1
]}

Wang, Yuanfang ^{[1
]}

Peng, Hao ^{[1
]}

Deng, Yangxi ^{[1
]}

Guo, Yingjie ^{[1
]}

Lu, Manjiao ^{[1
]}

Gan, Weidong ^{[1
]}

Peng, Tao ^{[2
,3
]}

Li, Meili ^{[1
]}

机构：

[1] Guangzhou Med Univ, Guangdong Prov Key Lab Allergy & Clin Immunol, Qingyuan Peoples Hosp,Affiliated Hosp 2,Affiliate, Sino French Hoffmann Inst,Sch Basic Med Sci, Guangzhou 510260, Guangdong, Peoples R China

[2] Guangzhou Med Univ, Sch Basic Med Sci, Sino French Hoffmann Inst, State Key Lab Resp Dis, Guangzhou 511436, Guangdong, Peoples R China

[3] South China Vaccine Corp Ltd, Guangzhou Sci Pk, Guangzhou 510663, Guangdong, Peoples R China

来源：

AGING-US | 2020年 / 12卷 / 07期

基金：

中国国家自然科学基金;

关键词：

HSV-1; UL6; nuclear import; importin; Ran-GTP; PUTATIVE TERMINASE SUBUNITS; PORTAL PROTEIN; EXPORT SIGNALS; TRANSPORT MECHANISM; LEUCINE-ZIPPER; TYPE-1; DNA; ALPHA; IDENTIFICATION; DETERMINANTS;

D O I：

10.18632/aging.102965

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

As an indispensable structure protein, the herpes simplex virus 1 (HSV-1) UL6 has been described to exert numerous roles in viral proliferation. However, its exact subcellular localization and subcellular transport mechanism is not well known. In the present study, by utilizing confocal fluorescent microscopy, UL6 was shown to mainly locate in the nucleus in enhanced yellow fluorescent protein or Flag tag fused expression plasmid-transfected cells or HSV-1-infected cells, whereas its predicted nuclear localization signal was nonfunctional. In addition, by exploiting dominant negative mutant and inhibitor of different nuclear import receptors, as well as co-immunoprecipitation and RNA interference assays, UL6 was established to interact with importin alpha 1, importin alpha 7 and transportin-1 to mediate its nuclear translocation under the help of Ran-mediated GTP hydrolysis. Accordingly, these results will advance the knowledge of UL6-mediated biological significances in HSV-1 infection cycle.

引用

页码：5751 / 5763

页数：13

共 48 条

[1] Disulfide Bond Formation in the Herpes Simplex Virus 1 UL6 Protein Is Required for Portal Ring Formation and Genome Encapsidation [J].