scholarly journals Special issue: Plant viruses. Movement proteins of plant viruses.

Uirusu ◽  
1994 ◽  
Vol 44 (1) ◽  
pp. 11-17
Author(s):  
Yuichiro Watanabe
Keyword(s):  
Plant Viruses ◽  
Special Issue ◽  
Movement Proteins

scholarly journals Leaf Plasmodesmata Respond Differently to TMV, ToBRFV and TYLCV Infection

Plants ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1442
Author(s):  
Yaarit Kutsher ◽  
Dalia Evenor ◽  
Eduard Belausov ◽  
Moshe Lapidot ◽  
Moshe Reuveni
Keyword(s):  
Cell Types ◽  
Plant Viruses ◽  
Tomato Leaf ◽  
Visual Localization ◽  
Tobacco Leaf ◽  
Signal Distribution ◽  
Movement Proteins ◽  
Significant Difference ◽  
Intracellular Mechanism ◽  
Leaf Curl Virus

Macromolecule and cytosolic signal distribution throughout the plant employs a unique cellular and intracellular mechanism called plasmodesmata (PD). Plant viruses spread throughout plants via PD using their movement proteins (MPs). Viral MPs induce changes in plasmodesmata’s structure and alter their ability to move macromolecule and cytosolic signals. The developmental distribution of a family member of proteins termed plasmodesmata located proteins number 5 (PDLP5) conjugated to GFP (PDLP5-GFP) is described here. The GFP enables the visual localization of PDLP5 in the cell via confocal microscopy. We observed that PDLP5-GFP protein is present in seed protein bodies and immediately after seed imbibition in the plasma membrane. The effect of three different plant viruses, the tobacco mosaic virus (TMV), tomato brown rugose fruit virus (ToBRFV, tobamoviruses), and tomato yellow leaf curl virus (TYLCV, begomoviruses), on PDLP5-GFP accumulation at the plasmodesmata was tested. In tobacco leaf, TMV and ToBRFV increased PDLP5-GFP amount at the plasmodesmata of cell types compared to control. However, there was no statistically significant difference in tomato leaf. On the other hand, TYLCV decreased PDLP5-GFP quantity in plasmodesmata in all tomato leaf cells compared to control, without any significant effect on plasmodesmata in tobacco leaf cells.

scholarly journals The Potato Virus X TGBp2 Protein Plays Dual Functional Roles in Viral Replication and Movement

2018 ◽  
Vol 93 (5) ◽  
Author(s):  
Xiaoyun Wu ◽  
Jiahui Liu ◽  
Mengzhu Chai ◽  
Jinhui Wang ◽  
Dalong Li ◽  
...  
Keyword(s):  
Triple Gene Block ◽  
Potato Virus X ◽  
Plant Viruses ◽  
Open Reading Frames ◽  
Movement Proteins ◽  
Gene Block ◽  
Functional Roles ◽  
Viral Rdrp ◽  
Dual Functional ◽  
Intercellular Movement

ABSTRACTPlant viruses usually encode one or more movement proteins (MP) to accomplish their intercellular movement. A group of positive-strand RNA plant viruses requires three viral proteins (TGBp1, TGBp2, and TGBp3) that are encoded by an evolutionarily conserved genetic module of three partially overlapping open reading frames (ORFs), termed the triple gene block (TGB). However, how these three viral movement proteins function cooperatively in viral intercellular movement is still elusive. Using a novelin vivodouble-stranded RNA (dsRNA) labeling system, we showed that the dsRNAs generated by potato virus X (PVX) RNA-dependent RNA polymerase (RdRp) are colocalized with viral RdRp, which are further tightly covered by “chain mail”-like TGBp2 aggregates and localizes alongside TGBp3 aggregates. We also discovered that TGBp2 interacts with the C-terminal domain of PVX RdRp, and this interaction is required for the localization of TGBp3 and itself to the RdRp/dsRNA bodies. Moreover, we reveal that the central and C-terminal hydrophilic domains of TGBp2 are required to interact with viral RdRp. Finally, we demonstrate that knockout of the entire TGBp2 or the domain involved in interacting with viral RdRp attenuates both PVX replication and movement. Collectively, these findings suggest that TGBp2 plays dual functional roles in PVX replication and intercellular movement.IMPORTANCEMany plant viruses contain three partially overlapping open reading frames (ORFs), termed the triple gene block (TGB), for intercellular movement. However, how the corresponding three proteins coordinate their functions remains obscure. In the present study, we provided multiple lines of evidence supporting the notion that PVX TGBp2 functions as the molecular adaptor bridging the interaction between the RdRp/dsRNA body and TGBp3 by forming “chain mail”-like structures in the RdRp/dsRNA body, which can also enhance viral replication. Taken together, our results provide new insights into the replication and movement of PVX and possibly also other TGB-containing plant viruses.

scholarly journals Introduction to Special Issue of Molecular Plant Pathology ‐ “Extracellular and intracellular perception of plant viruses”

2019 ◽  
Vol 20 (9) ◽  
pp. 1183-1184
Author(s):  
Miguel A. Aranda ◽  
Kristiina Mäkinen ◽  
Jeanmarie Verchot
Keyword(s):  
Plant Pathology ◽  
Plant Viruses ◽  
Special Issue

scholarly journals Special Issue: “The Complexity of the Potyviral Interaction Network”

Viruses ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 874
Author(s):  
Sylvie German-Retana ◽  
Kristiina Mäkinen
Keyword(s):  
Interaction Network ◽  
Plant Viruses ◽  
Crop Plants ◽  
Yield Losses ◽  
Special Issue ◽  
Potyvirus Species

Many potyvirus species are among the most economically-significant plant viruses as they cause substantial yield losses to crop plants globally [...]

scholarly journals The Plasmodesmal Localization Signal of TMV MP Is Recognized by Plant Synaptotagmin SYTA

mBio ◽  
2018 ◽  
Vol 9 (4) ◽  
Author(s):  
Cheng Yuan ◽  
Sondra G. Lazarowitz ◽  
Vitaly Citovsky
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Plant Cell Wall ◽  
Plant Viruses ◽  
Host Factor ◽  
Bimolecular Fluorescence Complementation ◽  
Host Recognition ◽  
Movement Proteins ◽  
Membrane Contact Sites ◽  
Localization Signal

ABSTRACT Plant viruses cross the barrier of the plant cell wall by moving through intercellular channels, termed plasmodesmata, to invade their hosts. They accomplish this by encoding movement proteins (MPs), which act to alter plasmodesmal gating. How MPs target to plasmodesmata is not well understood. Our recent characterization of the first plasmodesmal localization signal (PLS) identified in a viral MP, namely, the MP encoded by the Tobamovirus Tobacco mosaic virus (TMV), now provides the opportunity to identify host proteins that recognize this PLS and may be important for its plasmodesmal targeting. One such candidate protein is Arabidopsis synaptotagmin A (SYTA), which is required to form endoplasmic reticulum (ER)-plasma membrane contact sites and regulates the MP-mediated trafficking of begomoviruses, tobamoviruses, and potyviruses. In particular, SYTA interacts with, and regulates the cell-to-cell transport of, both TMV MP and the MP encoded by the Tobamovirus Turnip vein clearing virus (TVCV). Using in planta bimolecular fluorescence complementation (BiFC) and yeast two-hybrid assays, we show here that the TMV PLS interacted with SYTA. This PLS sequence was both necessary and sufficient for interaction with SYTA, and the plasmodesmal targeting activity of the TMV PLS was substantially reduced in an Arabidopsis syta knockdown line. Our findings show that SYTA is one host factor that can recognize the TMV PLS and suggest that this interaction may stabilize the association of TMV MP with plasmodesmata. IMPORTANCE Plant viruses use their movement proteins (MPs) to move through host intercellular connections, plasmodesmata. Perhaps one of the most intriguing, yet least studied, aspects of this transport is the MP signal sequences and their host recognition factors. Recently, we have described the plasmodesmal localization signal (PLS) of the Tobacco mosaic virus (TMV) MP. Here, we identified the Arabidopsis synaptotagmin A (SYTA) as a host factor that recognizes TMV MP PLS and promotes its association with the plasmodesmal membrane. The significance of these findings is two-fold: (i) we identified the TMV MP association with the cell membrane at plasmodesmata as an important PLS-dependent step in plasmodesmal targeting, and (ii) we identified the plant SYTA protein that specifically recognizes PLS as a host factor involved in this step.

scholarly journals Family Level Phylogenies Reveal Relationships of Plant Viruses within the Order Bunyavirales

Viruses ◽  
2020 ◽  
Vol 12 (9) ◽  
pp. 1010
Author(s):  
Venura Herath ◽  
Gustavo Romay ◽  
Cesar D. Urrutia ◽  
Jeanmarie Verchot
Keyword(s):  
Phylogenetic Analyses ◽  
Plant Viruses ◽  
Untranslated Regions ◽  
Rna Dependent Rna Polymerase ◽  
Movement Proteins ◽  
Phylogeny Analysis ◽  
Viral Movement ◽  
Family Level ◽  
Negative Sense ◽  
N Proteins

Bunyavirales are negative-sense segmented RNA viruses infecting arthropods, protozoans, plants, and animals. This study examines the phylogenetic relationships of plant viruses within this order, many of which are recently classified species. Comprehensive phylogenetic analyses of the viral RNA dependent RNA polymerase (RdRp), precursor glycoprotein (preGP), the nucleocapsid (N) proteins point toward common progenitor viruses. The RdRp of Fimoviridae and Tospoviridae show a close evolutional relationship while the preGP of Fimoviridae and Phenuiviridae show a closed relationship. The N proteins of Fimoviridae were closer to the Phasmaviridae, the Tospoviridae were close to some Phenuiviridae members and the Peribunyaviridae. The plant viral movement proteins of species within the Tospoviridae and Phenuiviridae were more closely related to each other than to members of the Fimoviridae. Interestingly, distal ends of 3′ and 5′ untranslated regions of species within the Fimoviridae shared similarity to arthropod and vertebrate infecting members of the Cruliviridae and Peribunyaviridae compared to other plant virus families. Co-phylogeny analysis of the plant infecting viruses indicates that duplication and host switching were more common than co-divergence with a host species.

scholarly journals Replication and trafficking of a plant virus are coupled at the entrances of plasmodesmata

2013 ◽  
Vol 201 (7) ◽  
pp. 981-995 ◽  
Author(s):  
Jens Tilsner ◽  
Olga Linnik ◽  
Marion Louveaux ◽  
Ian M. Roberts ◽  
Sean N. Chapman ◽  
...  
Keyword(s):  
Plant Virus ◽  
Plant Cell Wall ◽  
Triple Gene Block ◽  
Potato Virus X ◽  
Plant Viruses ◽  
Viral Coat Protein ◽  
Movement Proteins ◽  
Gene Block ◽  
Replication Sites ◽  
Viral Coat

Plant viruses use movement proteins (MPs) to modify intercellular pores called plasmodesmata (PD) to cross the plant cell wall. Many viruses encode a conserved set of three MPs, known as the triple gene block (TGB), typified by Potato virus X (PVX). In this paper, using live-cell imaging of viral RNA (vRNA) and virus-encoded proteins, we show that the TGB proteins have distinct functions during movement. TGB2 and TGB3 established endoplasmic reticulum–derived membranous caps at PD orifices. These caps harbored the PVX replicase and nonencapsidated vRNA and represented PD-anchored viral replication sites. TGB1 mediated insertion of the viral coat protein into PD, probably by its interaction with the 5′ end of nascent virions, and was recruited to PD by the TGB2/3 complex. We propose a new model of plant virus movement, which we term coreplicational insertion, in which MPs function to compartmentalize replication complexes at PD for localized RNA synthesis and directional trafficking of the virus between cells.

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