DEVELOPMENTALLY REGULATED PLASMA MEMBRANE PROTEIN of Nicotiana benthamiana contributes to potyvirus movement and transports to plasmodesmata via the early secretory pathway and the actomyosin system

• Published in: Plant physiology (Bethesda) Vol. 167; no. 2; pp. 394 - 410
• Main Authors: Geng, Chao, Cong, Qian-Qian, Li, Xiang-Dong, Mou, An-Li, Gao, Rui, Liu, Jin-Liang, Tian, Yan-Ping
• Format: Journal Article
• Language: English
• Published: United States 01.02.2015
• Subjects: Actin Cytoskeleton - drug effects; Actin Cytoskeleton - metabolism; Actomyosin - metabolism; Amino Acid Sequence; Brefeldin A - pharmacology; Bridged Bicyclo Compounds, Heterocyclic - pharmacology; Gene Silencing - drug effects; Green Fluorescent Proteins - metabolism; Models, Biological; Molecular Sequence Data; Movement - drug effects; Mutation; Myosins - metabolism; Nicotiana - drug effects; Nicotiana - metabolism; Plant Diseases - virology; Plant Proteins - metabolism; Plasmodesmata - drug effects; Plasmodesmata - metabolism; Potyvirus - pathogenicity; Protein Binding - drug effects; Protein Structure, Tertiary; Protein Transport - drug effects; Recombinant Fusion Proteins - metabolism; Saccharomyces cerevisiae - metabolism; Secretory Pathway - drug effects; Subcellular Fractions - drug effects; Subcellular Fractions - metabolism; Thiazolidines - pharmacology; Viral Proteins - chemistry; Viral Proteins - metabolism
• ISSN: 1532-2548; 1532-2548
• DOI: 10.1104/pp.114.252734

The intercellular movement of plant viruses requires both viral and host proteins. Previous studies have demonstrated that the frame-shift protein P3N-PIPO (for the protein encoded by the open reading frame [ORF] containing 5'-terminus of P3 and a +2 frame-shift ORF called Pretty Interesting Potyviridae ORF and embedded in the P3) and CYLINDRICAL INCLUSION (CI) proteins were required for potyvirus cell-to-cell movement. Here, we provide genetic evidence showing that a Tobacco vein banding mosaic virus (TVBMV; genus Potyvirus) mutant carrying a truncated PIPO domain of 58 amino acid residues could move between cells and induce systemic infection in Nicotiana benthamiana plants; mutants carrying a PIPO domain of seven, 20, or 43 amino acid residues failed to move between cells and cause systemic infection in this host plant. Interestingly, the movement-defective mutants produced progeny that eliminated the previously introduced stop codons and thus restored their systemic movement ability. We also present evidence showing that a developmentally regulated plasma membrane protein of N. benthamiana (referred to as NbDREPP) interacted with both P3N-PIPO and CI of the movement-competent TVBMV. The knockdown of NbDREPP gene expression in N. benthamiana impeded the cell-to-cell movement of TVBMV. NbDREPP was shown to colocalize with TVBMV P3N-PIPO and CI at plasmodesmata (PD) and traffic to PD via the early secretory pathway and the actomyosin motility system. We also show that myosin XI-2 is specially required for transporting NbDREPP to PD. In conclusion, NbDREPP is a key host protein within the early secretory pathway and the actomyosin motility system that interacts with two movement proteins and influences virus movement.