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.
journal_name
Virologyjournal_title
Virologyauthors
Andika IB,Zheng S,Tan Z,Sun L,Kondo H,Zhou X,Chen Jdoi
10.1016/j.virol.2012.10.024subject
Has Abstractpub_date
2013-01-20 00:00:00pages
493-503issue
2eissn
0042-6822issn
1096-0341pii
S0042-6822(12)00532-6journal_volume
435pub_type
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