The Bacillus thuringiensis crystal protein Cry1Aa is normally selectively active to caterpillar larvae. Through rational design, toxicity (microg/ml) to the mosquito Culex pipiens was introduced by selected deletions and substitutions of the loop residues of domain II. Toxicity to its natural target Manduca sexta was concomitantly abolished. The successful grafting of the alternate mosquito toxicity onto the original lepidopteran Cry1Aa toxin demonstrates the possibility of designing and engineering a desired toxicity into any toxin of a common scaffold by reshaping the receptor binding region with desired specificities.

Redesigning Bacillus thuringiensis Cry1Aa Toxin into a Mosquito Toxin

Laccases belonging to multicopper oxidase family oxidize a broad range of reducing substrates, especially industrial effluents-derived polyphenols, which causing major effect on human health as well as environment. In order to investigate the molecular mechanism of interaction between laccase and its substrate, it is a good idea to analyze three-dimensional structure of laccase. Based on crystal structure of Escherichia coli laccase CueO, the three-dimensional structure of Aeromonas hydrophila Laccase (Ah-lac) was constructed by homology modeling and further evaluated using PROSA energy and ERRAT. The substrate binding site in Ah-lac was predicted and the binding mode of 2,5-Xylidine as a putative ligand to Ah-lac was presented using molecular docking. The residues of Met378 and His382 in the binding pocket are responsible for the interactions with 2,5-Xylidine via two hydrogen bonds. The two residues could be important for substrate recognition.

Homology Modeling of Aeromonas hydrophila Laccase and its Molecular Docking with the 2,5-Xylidine

Activated toxins interact with α-amylase receptor on the brush border membrane vesicle (BBMV) of the midgut epithelium, which activates intracellular oncotic pathways and leads to cell death. In order to decipher the mechanism of process how toxins interact with their receptors, it is essential to investigate their three-dimensional structure. The three-dimensional structure of α-amylase was constructed by homology modeling, based on crystal structure of Bacillus cereus oligo-1,6-glucosidase and the model was further evaluated using PROSA energy and ERRAT. The substrate binding pocket responsible for the interactions with toxins was predicted and analyzed, and the important role of binding of toxin to binding pocket on α-amylase was discussed in the aspect of Cry4Ba and Cry11Aa toxicity.

Sequence Analysis and Functional Interpretation of α-Amylase Receptor from Anopheles albimanus Using a Molecular Model

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Homology Modeling of Aeromonas hydrophila Laccase and its Molecular Docking with the 2,5-Xylidine

Sequence Analysis and Functional Interpretation of α-Amylase Receptor from Anopheles albimanus Using a Molecular Model