RESUMO
An understanding of virus disassembly requires a detailed understanding of the protein-protein and protein-nucleic acid interactions which stabilize the virion. We have characterized a mutant of cowpea chlorotic mottle virus [cpR26C (coat protein R26C)] that displays increased virion stability and is abnormal in virion disassembly when purified under nonreducing conditions. Reduced virions are infectious, whereas nonreduced virions are noninfectious. The cpR26C mutant virions purified under nonreducing conditions resist disassembly in 0.5 M CaCl2, pH 7.5. The nonreduced cpR26C mutant virions swell in neutral pH conditions (pH 7.5) but do not disassociate when the ionic strength is increased. In contrast, wild-type virions or cpR26C mutant virions isolated under reducing conditions completely disassociate into the RNA and capsid protein components at pH 7.5 and high ionic strength (i > 1.0). Sequence analysis of the cpR26C mutant identified a single C to U nucleotide change at position 1435 of RNA 3 (position 86 of RNA 4), which results in a arginine to cysteine change at position 26 of the coat protein. The cpR26C mutant provides an ideal chemical switch for examining virion assembly and disassembly.