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Nucleo-cytoplasmic shuttling of VPg encoded by Wheat yellow mosaic virus requires association with the coat protein

文献类型： 外文期刊

作者： Sun, Liying 1 ; Jing, Bian 2 ; Andika, Ida Bagus 1 ; Hu, Yingchun 3 ; Sun, Bingjian 4 ; Xiang, Rong 2 ; Kondo, Hideki; 1 ;

作者机构： 1.Zhejiang Acad Agr Sci, Inst Virol & Biotechnol, Minist Agr,Key Lab Biotechnol Plant Protect, State Key Lab Breeding Base Zhejiang Sustainable, Hangzhou 310021, Zhejiang, Peoples R China

2.Zhejiang Normal Univ, Coll Chem & Life Sci, Jinhua 321004, Peoples R China

3.Peking Univ, Coll Life Sci, Minist Educ Cell Proliferat & Different, Key Lab, Beijing 100871, Peoples R China

4.Henan Agr Univ, Coll Plant Protect, Zhengzhou 450002, Henan Province, Peoples R China

5.Okayama Univ, Inst Plant Sci & Resources, Kurashiki, Okayama 7100046, Japan

关键词： Nucleo-cytoplasmic shuttling;requires association;protein

期刊名称：JOURNAL OF GENERAL VIROLOGY （ 影响因子：3.891； 五年影响因子：3.719 ）

ISSN：

年卷期：

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收录情况： SCI

摘要： VPg (virus protein, genome-linked) is a multifunctional protein that plays important roles in viral multiplication in the cytoplasm. However, a number of VPgs encoded by plant viruses target the nucleus and this appears to be biologically significant. These VPgs may therefore be translocated between nuclear and cytoplasmic compartments during virus infection, but such nucleo-cytoplasmic transport has not been demonstrated. We report that VPg encoded by Wheat yellow mosaic virus (WYMV, genus Bymovirus, family Potyviridae) accumulated in both the nucleus and cytoplasm of infected cells, but localized exclusively in the nucleus when expressed alone in plants. Computational analyses predicted the presence of a nuclear localization signal (NLS) and a nuclear export signal (NES) in WYMV VPg. Mutational analyses showed that both the N-terminal and the NLS domains of VPg contribute to the efficiency of nuclear targeting. In vitro and in planta assays indicated that VPg interacts with WYMV coat protein (CP) and proteinase 1 (P1) proteins. Observation of VPg fused to a fluorescent protein and subcellular fractionation experiments showed that VPg was translocated to the cytoplasm when co-expressed with CP, but not with P1. Mutations in the NES domain or treatment with leptomycin B prevented VPg translocation to the cytoplasm when co-expressed with CP. Our results suggest that association with CP facilitates the nuclear export of VPg during WYMV infection.

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