AI Article Synopsis
- The binary toxin from Bacillus sphaericus consists of two proteins, BinA and BinB, with BinB determining specificity and BinA expected to be responsible for toxic action after penetrating cells.
- Substituting cysteine residues in BinA with alanine and serine revealed that Cys195 reduced toxicity while substitutions at Cys31 and Cys47 completely abolished it.
- This study is the first to show that specific cysteine residues in BinA are essential for the full toxicity of the binary toxin, suggesting they are crucial for the interaction and formation of the active complex with BinB.
Article Abstract
The mosquito larvicidal binary toxin produced by Bacillus sphaericus is composed of 2 proteins called BinA and BinB. While BinB acts as specificity determinant, BinA is expected to bind to BinB, translocates into cytosol, and exerts its activity via an unknown mechanism. To study the role of cysteine in BinA, 3 cysteine residues were substituted by alanine and serine. Substitution at Cys195 significantly reduced the toxin activity, whereas substitution at Cys31 and Cys47 abolished its toxicity. Intrinsic fluorescent analysis suggested that all mutant proteins should have similar tertiary structure to that of the wild type. Analysis of the mutant protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with and without a reducing agent indicated that all 3 cysteine residues were not involved in disulfide bond formation within the BinA molecule. This is the first report to demonstrate that cysteine residues at 3 positions in BinA are required for full toxicity of the binary toxin. They may play a critical role during oligomerization or interaction between BinA and BinB to form the active complex.
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| http://dx.doi.org/10.1007/s00284-007-9065-9 | DOI Listing |
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