The charged residues in the surface-exposed C-terminus of the Soybean mosaic virus coat protein are critical for cell-to-cell movement.
The Soybean mosaic virus (SMV) coat protein (CP) is necessary for virion assembly and viral cell-to-cell and long-distance movements in plants. We previously showed that the C-terminal region of the SMV CP is required for CP self-interaction. In the present study, we generated SMV mutants containing CPs with single amino acid substitutions of the charged amino acids in the C-proximal region. Infectivity and cell-to-cell movement of the SMV mutants were examined in soybean plants. Through this genetic approach, we identified three charged amino acid residues (R245, H246, and D250) in the surface-exposed C-terminus of the SMV CP that are critical for virus cell-to-cell and long-distance movement. Our findings suggest that the identified charged amino acids in the surface-exposed C-terminus of SMV CP are critical for CP intersubunit interactions and thereby for cell-to-cell and long-distance movement and virion assembly.
Department of Agricultural Biotechnology and Plant Genomics and Breeding Institute, Seoul National University, Seoul 151-921, Republic of Korea; Crop Protection Division, National Academy of Agricultural Science, Rural Development Administration, Suwon 441-707, Republic of Korea.
Jang-Kyun
JK
Seo
Mi Sa
MS
Vo Phan
Sung-Hwan
SH
Kang
Hong-Soo
HS
Choi
Kook-Hyung
KH
Kim
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000596:Amino Acids / Q000235:genetics / Q000378:metabolism*; D036022:Capsid Proteins / Q000235:genetics / Q000378:metabolism*; D004252:DNA Mutational Analysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017800:Potyvirus / Q000235:genetics / Q000502:physiology*; D011487:Protein Conformation; D013025:Glycine max / Q000821:virology; D053586:Virus Internalization; D057074:Virus Release
D000596:Amino Acids; D036022:Capsid Proteins
Coat protein; Movement; Potyvirus; SMV; Virion assembly