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Endoplasmic reticulum export and vesicle formation of the movement protein of Chinese wheat mosaic virus are regulated by two transmembrane domains and depend on the secretory pathway

文献类型: 外文期刊

作者: Andika, Ida Bagus 2 ; Zheng, Shiling 1 ; Tan, Zilong 3 ; Sun, Liying 2 ; Kondo, Hideki 4 ; Zhou, Xueping 1 ; Chen, Jia 1 ;

作者机构: 1.Zhejiang Univ, Inst Biotechnol, State Key Lab Rice Biol, Hangzhou 310003, Zhejiang, Peoples R China

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

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

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

关键词: 30K superfamily;Cell-to-cell movement;Chinese wheat mosaic virus;Endoplasmic reticulum;Furovirus;Movement-protein;Plasmodesmata;Transmembrane domain;Vesicles

期刊名称:VIROLOGY ( 影响因子:3.616; 五年影响因子:3.967 )

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收录情况: SCI

摘要: The 37K protein of Chinese wheat mosaic virus (CWMV) belongs to the 30K superfamily of plant virus movement proteins. CWMV 37K trans-complemented the cell-to-cell spread of a movement-defective Potato virus X. CWMV 37K fused to enhanced green fluorescent protein localized to plasmodesmata and formed endoplasmic reticulum (ER)-derived vesicular and large aggregate structures. CWMV 37K has two putative N-terminal transmembrane domains (TMDs). Mutations disrupting TMD1 or TMD2 impaired 37K movement function; those mutants were unable to form ER-derived structures but instead accumulated in the ER. Treatment with Brefeldin A or overexpression of the dominant negative mutant of Sar1 retained 37K in the ER, indicating that ER export of 37K is dependent on the secretory pathway. Moreover, CWMV 37K interacted with pectin methylesterases and mutations in TMD1 or TMD2 impaired this interaction in planta. The results suggest that the two TMDs regulate the movement function and intracellular transport of 37K.

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