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 59-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 movementdefective 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.

Dissecting the Molecular Mechanism of the Subcellular Localization and Cell-to-cell Movement of the Sugarcane mosaic virus P3N-PIPO

“…Latrunculin B (Lat B) and Brefeldin A (BFA) interfere with cellular processes and have been used to investigate viral intracellular trafficking 21 , 26 . Lat B is a chemical inhibitor of actin polymerization 34 .…”

“…Among these 11 proteins, CP, CI, HC-Pro, VPg, 6K2 and P3N-PIPO are involved in viral cell-to-cell movement 20 – 25 . Accumulating evidence suggests that P3N-PIPO functions as an MP in Potyviridae 17 , 21 , 22 , 26 – 28 . For example, synonymous mutations in the P3 cistron that altered the pipo open reading frame (ORF) of Wheat streak mosaic virus disrupted the virus movement in plants 28 .…”

Remorin interacting with PCaP1 impairs Turnip mosaic virus intercellular movement but is antagonised by VPg

“…Considering that TuMV is synergistic with Cucumber mosaic virus (CMV) and promotes the cell‐to‐cell movement of the transport‐deficient isolate CMV‐Y (Takeshita & Takanami, ), we speculate that PD actin filament depolymerisation may contribute to this synergism. The homologues of PCaP1 not only interact with the P3N‐PIPO of TuMV (Vijayapalani et al ., ) but also those of Tobacco vein banding mosaic virus (Geng et al ., ) or Sugarcane mosaic virus (Cheng et al ., ), which implicates a general requirement for PCaP1 in potyviral cell‐to‐cell movement. However, TuMV eventually establishes systemic infection in pcap1 (Vijayapalani et al ., ) or P PCaP1 :PCaP1 N5A ; pcap1 in the present work, indicating that PCaP1 may be involved in the early stage of TuMV infection, or other actin filament‐severing proteins are involved in TuMV infection.…”

Identification for soybean host factors interacting with P3N-PIPO protein of Soybean mosaic virus

“…Previously, the host proteins which interact with potyviral proteins were identified for P1, HC-Pro, CP, CI, nuclear inclusion protein b and viral genome-linked protein using the yeast two-hybrid system (Gao et al 2012). Recent reports have described the interaction between a cationbinding protein, PCaP1, which attaches to the plasma membrane in A. thaliana infected with Turnip mosaic virus (Vijayapalani et al 2012), and a developmentally regulated plasma membrane protein, NbDREPP, in N. benthamiana infected with Tobacco vein banding mosaic virus (Geng et al 2015). However, the information has not been reported of the host proteins that interact with SMV P3N-PIPO.…”