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 ◽  
...  

2020 ◽  
Vol 94 (8) ◽  
Author(s):  
Mengzhu Chai ◽  
Xiaoyun Wu ◽  
Jiahui Liu ◽  
Yue Fang ◽  
Yameng Luan ◽  
...  

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.





1994 ◽  
Vol 141 (2) ◽  
pp. 186-194
Author(s):  
G. Boudazin ◽  
C. Vergnet ◽  
B. Gélie ◽  
M. Meyer ◽  
J. Grosclaude ◽  
...  


2013 ◽  
Vol 9 (10) ◽  
pp. e1003683 ◽  
Author(s):  
Maxime Agbeci ◽  
Romain Grangeon ◽  
Richard S. Nelson ◽  
Huanquan Zheng ◽  
Jean-François Laliberté


2008 ◽  
Vol 89 (3) ◽  
pp. 829-838 ◽  
Author(s):  
Rasa Gabrenaite-Verkhovskaya ◽  
Igor A. Andreev ◽  
Natalia O. Kalinina ◽  
Lesley Torrance ◽  
Michael E. Taliansky ◽  
...  

Potato virus A (PVA) particles were purified by centrifugation through a 30 % sucrose cushion and the pellet (P1) was resuspended and sedimented through a 5–40 % sucrose gradient. The gradient separation resulted in two different virus particle populations: a virus fraction (F) that formed a band in the gradient and one that formed a pellet (P2) at the bottom of the gradient. All three preparations contained infectious particles that retained their integrity when visualized by electron microscopy (EM). Western blotting of the P1 particles revealed that the viral RNA helicase, cylindrical inclusion protein (CI), co-purified with virus particles. This result was confirmed with co-immunoprecipitation experiments. CI was detected in P2 particle preparations, whereas F particles were devoid of detectable amounts of CI. ATPase activity was detected in all three preparations with the greatest amount in P2. Results from immunogold-labelling EM experiments suggested that a fraction of the CI present in the preparations was localized to one end of the virion. Atomic force microscopy (AFM) studies showed that P1 and P2 contained intact particles, some of which had a protruding tip structure at one end, whilst F virions were less stable and mostly appeared as beaded structures under the conditions of AFM. The RNA of the particles in F was translated five to ten times more efficiently than RNA from P2 particles when these preparations were subjected to translation in wheat-germ extracts. The results are discussed in the context of a model for CI-mediated functions.



2020 ◽  
Vol 21 (9) ◽  
pp. 1194-1211 ◽  
Author(s):  
Zhaoji Dai ◽  
Rongrong He ◽  
Mark A. Bernards ◽  
Aiming Wang




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