title: Packaging and structural phenotype of brome mosaic virus capsid protein with altered N-terminal β-hexamer structure.
abstract: The first 45 amino acid region of brome mosaic virus (BMV) capsid protein (CP) contains RNA binding and structural domains that are implicated in the assembly of infectious virions. One such important structural domain encompassing amino acids 28QPVIV32, highly conserved between BMV and cowpea chlorotic mottle virus (CCMV), exhibits a β-hexamer structure. In this study we report that alteration of the β-hexamer structure by mutating 28QPVIV32 to 28AAAAA32 had no effect either on symptom phenotype, local and systemic movement in Chenopodium quinoa and RNA profile of in vivo assembled virions. However, sensitivity to RNase and assembly phenotypes distinguished virions assembled with CP subunits having β-hexamer from those of wild type. A comparison of 3-D models obtained by cryo electron microscopy revealed overall similar structural features for wild type and mutant virions, with small but significant differences near the 3-fold axes of symmetry.
authors.affiliation: Department of Plant Pathology and Microbiology, University of California, Riverside, CA 92521-0122, USA.
authors.forename: Melissanne
authors.initials: M
authors.lastname: de Wispelaere
authors.forename: Sonali
authors.initials: S
authors.lastname: Chaturvedi
authors.forename: Stephan
authors.initials: S
authors.lastname: Wilkens
authors.forename: A L N
authors.initials: AL
authors.lastname: Rao
mesh_terms: D019943:Amino Acid Substitution; D017795:Bromovirus / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D027465:Chenopodium quinoa / Q000821:virology*; D020285:Cryoelectron Microscopy; D005838:Genotype; D008958:Models, Molecular; D008968:Molecular Conformation; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010641:Phenotype; D010935:Plant Diseases / Q000821:virology; D055503:Protein Multimerization; D012367:RNA, Viral / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019065:Virus Assembly
chemical_list: D036022:Capsid Proteins; D050505:Mutant Proteins; D012367:RNA, Viral; D016601:RNA-Binding Proteins