The primary structure of cowpea chlorotic mottle virus coat protein

Abstract

The amino acid sequence of the coat protein of wild-type cowpea chlorotic mottle virus has been nearly completely determined by direct methods. The sites of amino acid replacements were identified in the coat proteins of an oxidation-sensitive mutant, a temperature-sensitive mutant, and a salt-stable mutant. The replacements are a cysteinyl residue for the arginyl residue at position 25 in the oxidation-sensitive mutant, glutamic acid and alanine, respectively, for lysine and valine at positions 21 and 87 in the temperature-sensitive mutant, and arginine for lysine at position 105 in the salt-stable mutant. The substitutions are consistent with point mutations.