The C terminus of brome mosaic virus coat protein controls viral cell-to-cell and long-distance movement.
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.
Okinaka
Y
Y
Laboratory of Plant Pathology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
Mise
K
K
Suzuki
E
E
Okuno
T
T
Furusawa
I
I
D000409:Alanine; D019943:Amino Acid Substitution; D001692:Biological Transport; D017795:Bromovirus / Q000235:genetics / Q000472:pathogenicity*; D002213:Capsid / Q000235:genetics*; D001467:Hordeum; D016297:Mutagenesis, Site-Directed; D010935:Plant Diseases / Q000821:virology*; D010947:Plants, Toxic; D014026:Nicotiana
D000409:Alanine