Identification of a tobacco protein interacting with tomato mosaic virus coat protein and facilitating long-distance movement of virus

2005 ◽  
Vol 150 (10) ◽  
pp. 1993-2008 ◽  
Author(s):  
Y. Li ◽  
M. Y. Wu ◽  
H. H. Song ◽  
X. Hu ◽  
B. S. Qiu
PLoS ONE ◽  
2014 ◽  
Vol 9 (11) ◽  
pp. e113347 ◽  
Author(s):  
Shengniao Niu ◽  
Francisco M. Gil-Salas ◽  
Sunil Kumar Tewary ◽  
Ashwin Kuppusamy Samales ◽  
John Johnson ◽  
...  

2001 ◽  
Vol 75 (11) ◽  
pp. 5385-5390 ◽  
Author(s):  
Yasushi Okinaka ◽  
Kazuyuki Mise ◽  
Eri Suzuki ◽  
Tetsuro Okuno ◽  
Iwao Furusawa

ABSTRACT To investigate the functional domains of the coat protein (CP; 189 amino acids) of Brome mosaic virus, a plant RNA virus, 19 alanine-scanning mutants were constructed and tested for their infectivity in barley and Nicotiana benthamiana. Despite its apparent normal replicative competence and CP production, the C-terminal mutant F184A produced no virions. Furthermore, virion-forming C-terminal mutants P178A and D182A failed to move from cell to cell in both plant species, and mutants D181A and V187A showed host-specific movement. These results indicate that the C-terminal region of CP plays some important roles in virus movement and encapsidation. The specificity of certain mutations for viral movement in two different plant species is evidence for the involvement of host-specific factors.


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