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.

Abstract

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.

• Authors: Chao Geng, Qian-Qian Cong, Xiang-Dong Li, An-Li Mou, Rui Gao, Jin-Liang Liu, Yan-Ping Tian
• Journal: Plant physiology (Plant Physiol) Vol. 167 Issue 2 Pg. 394-410 (Feb 2015) ISSN: 1532-2548 [Electronic] United States
• PMID: 25540331 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: © 2015 American Society of Plant Biologists. All Rights Reserved.

Chemical References

• Bridged Bicyclo Compounds, Heterocyclic
• Plant Proteins
• Recombinant Fusion Proteins
• Thiazolidines
• Viral Proteins
• Green Fluorescent Proteins
• Brefeldin A
• Actomyosin
• Myosins
• latrunculin B

Topics

• Actin Cytoskeleton (drug effects, 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)
• Plant Diseases (virology)
• Plant Proteins (metabolism)
• Plasmodesmata (drug effects, 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, metabolism)
• Thiazolidines (pharmacology)
• Tobacco (drug effects, metabolism)
• Viral Proteins (chemistry, metabolism)