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

Ida Bagus Andika, Shiling Zheng, Zilong Tan, Liying Sun, Hideki Kondo, Xueping Zhou, Jianping Chen

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)493-503
Number of pages11
JournalVirology
Volume435
Issue number2
DOIs
Publication statusPublished - Jan 20 2013

Keywords

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

ASJC Scopus subject areas

  • Virology

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