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

2019 ◽  
Vol 225 (5) ◽  
pp. 2122-2139 ◽  
Author(s):  
Guangyuan Cheng ◽  
Zongtao Yang ◽  
Hai Zhang ◽  
Jisen Zhang ◽  
Jingsheng Xu
Keyword(s):  
Mosaic Virus ◽  
Turnip Mosaic Virus ◽  
Intercellular Movement

scholarly journals Contribution of Host Intracellular Transport Machineries to Intercellular Movement of Turnip Mosaic Virus

2013 ◽  
Vol 9 (10) ◽  
pp. e1003683 ◽  
Author(s):  
Maxime Agbeci ◽  
Romain Grangeon ◽  
Richard S. Nelson ◽  
Huanquan Zheng ◽  
Jean-François Laliberté
Keyword(s):  
Mosaic Virus ◽  
Intracellular Transport ◽  
Turnip Mosaic Virus ◽  
Intercellular Movement

scholarly journals The cis ‐expression of the coat protein of turnip mosaic virus is essential for viral intercellular movement in plants

2020 ◽  
Vol 21 (9) ◽  
pp. 1194-1211 ◽  
Author(s):  
Zhaoji Dai ◽  
Rongrong He ◽  
Mark A. Bernards ◽  
Aiming Wang
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Turnip Mosaic Virus ◽  
Intercellular Movement

scholarly journals P3N-PIPO Interacts with P3 via the Shared N-Terminal Domain To Recruit Viral Replication Vesicles for Cell-to-Cell Movement

2020 ◽  
Vol 94 (8) ◽  
Author(s):  
Mengzhu Chai ◽  
Xiaoyun Wu ◽  
Jiahui Liu ◽  
Yue Fang ◽  
Yameng Luan ◽  
...  
Keyword(s):  
Viral Replication ◽  
Mosaic Virus ◽  
Essential Role ◽  
Movement Protein ◽  
Cell Movement ◽  
Plant Viruses ◽  
Turnip Mosaic Virus ◽  
Limited Information ◽  
Intercellular Movement ◽  
Model Virus

ABSTRACT P3N-PIPO, the only dedicated movement protein (MP) of potyviruses, directs cylindrical inclusion (CI) protein from the cytoplasm to the plasmodesma (PD), where CI forms conical structures for intercellular movement. To better understand potyviral cell-to-cell movement, we further characterized P3N-PIPO using Turnip mosaic virus (TuMV) as a model virus. We found that P3N-PIPO interacts with P3 via the shared P3N domain and that TuMV mutants lacking the P3N domain of either P3N-PIPO or P3 are defective in cell-to-cell movement. Moreover, we found that the PIPO domain of P3N-PIPO is sufficient to direct CI to the PD, whereas the P3N domain is necessary for localization of P3N-PIPO to 6K2-labeled vesicles or aggregates. Finally, we discovered that the interaction between P3 and P3N-PIPO is essential for the recruitment of CI to cytoplasmic 6K2-containing structures and the association of 6K2-containing structures with PD-located CI inclusions. These data suggest that both P3N and PIPO domains are indispensable for potyviral cell-to-cell movement and that the 6K2 vesicles in proximity to PDs resulting from multipartite interactions among 6K2, P3, P3N-PIPO, and CI may also play an essential role in this process. IMPORTANCE Potyviruses include numerous economically important viruses that represent approximately 30% of known plant viruses. However, there is still limited information about the mechanism of potyviral cell-to-cell movement. Here, we show that P3N-PIPO interacts with and recruits CI to the PD via the PIPO domain and interacts with P3 via the shared P3N domain. We further report that the interaction of P3N-PIPO and P3 is associated with 6K2 vesicles and brings the 6K2 vesicles into proximity with PD-located CI structures. These results support the notion that the replication and cell-to-cell movement of potyviruses are processes coupled by anchoring viral replication complexes at the entrance of PDs, which greatly increase our knowledge of the intercellular movement of potyviruses.

scholarly journals Cylindrical Inclusion Protein of Turnip Mosaic Virus Serves as a Docking Point for the Intercellular Movement of Viral Replication Vesicles

2017 ◽  
Vol 175 (4) ◽  
pp. 1732-1744 ◽  
Author(s):  
Nooshin Movahed ◽  
Camilo Patarroyo ◽  
Jiaqi Sun ◽  
Hojatollah Vali ◽  
Jean-François Laliberté ◽  
...  
Keyword(s):  
Viral Replication ◽  
Mosaic Virus ◽  
Turnip Mosaic Virus ◽  
Cylindrical Inclusion ◽  
Inclusion Protein ◽  
Intercellular Movement ◽  
Cylindrical Inclusion Protein

scholarly journals Comparison of two Turnip mosaic virus P1 proteins in their ability to co-localize with the Arabidopsis thaliana G3BP-2 protein

Virus Genes ◽  
2021 ◽  
Vol 57 (2) ◽  
pp. 233-237
Author(s):  
Hendrik Reuper ◽  
Björn Krenz
Keyword(s):  
Arabidopsis Thaliana ◽  
Mosaic Virus ◽  
Specific Interaction ◽  
Viral Proteins ◽  
Turnip Mosaic Virus ◽  
Stress Conditions ◽  
C Terminus ◽  
Positive Sense ◽  
Key Factor ◽  
Large Host

AbstractTurnip mosaic virus (TuMV), belonging to the genus Potyvirus (family Potyviridae), has a large host range and consists of a single-stranded positive sense RNA genome encoding 12 proteins, including the P1 protease. This protein which is separated from the polyprotein by cis cleavage at its respective C-terminus, has been attributed with different functions during potyviral infection of plants. P1 of Turnip mosaic virus (P1-TuMV) harbors an FGSF-motif and FGSL-motif at its N-terminus. This motif is predicted to be a binding site for the host Ras GTPase-activating protein-binding protein (G3BP), which is a key factor for stress granule (SG) formation in mammalian systems and often targeted by viruses to inhibit SG formation. We therefore hypothesized that P1-TuMV might interact with G3BP to control and regulate plant SGs to optimize cellular conditions for the production of viral proteins. Here, we analyzed the co-localization of the Arabidopsis thaliana G3BP-2 with the P1 of two TuMV isolates, namely UK 1 and DEU 2. Surprisingly, P1-TuMV-DEU 2 co-localized with AtG3BP-2 under abiotic stress conditions, whereas P1-TuMV-UK 1 did not. AtG3BP-2::RFP showed strong SGs formation after stress, while P1-UK 1::eGFP maintained a chloroplastic signal under stress conditions, the signal of P1-DEU 2::eGFP co-localized with that of AtG3BP-2::RFP. This indicates a specific interaction between P1-DEU 2 and the AtG3BP family which is not solely based on the canonical interaction motifs.

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