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The two-component Cry48Aa/Cry49Aa toxin produced by Lysinibacillus sphaericus shows specifically toxic to Culex quinquefasciatus mosquito larvae. Cry49Aa C-terminal domain is responsible for specific binding to the larval gut cell membrane, while its N-terminal domain is required for interaction with Cry48Aa. To investigate functional role of cysteine in Cry49Aa, four cysteine residues at positions 70, 91, 183, and 258 were substituted by alanine. All mutants showed similar crystalline morphology and comparable yield to that of the wild type except that the yield of the C91A mutant was low. Four cysteine residues did not involve in disulfide bond formation within or between Cry49Aa molecules. Cys91, Cys183, and Cys258 are essential for larvicidal activity against C. quinquefasciatus larvae, while Cys70 is not. Substitution at C91, C183, and C258 caused weaker Cry48Aa- Cry49Aa interaction, while mutations at C183 and C258 reduced the binding capacities to the larval gut cell membrane. Thus, Cysteine residues at position 91, 183, and 258 in Cry49Aa are required for full toxicity of Cry48Aa/Cry49Aa toxin.

Cys183 and Cys258 in Cry49Aa toxin from Lysinibacillus sphaericus are essential for toxicity to Culex quinquefasciatus larvae