What question did this study set out to answer?

To determine whether replacing domain III of the Bacillus thuringiensis CryIA(b) toxin with that of CryIC improves toxicity toward Spodoptera exigua and alters gut membrane recognition.

May 1, 1996Applied and Environmental MicrobiologyOpen Access

Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition

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Authors

RMRuud A. de MaagdEuropean Food Safety Authority MKMarcel KwaEuropean Medicines Agency HKH van der KleiGhent University Hospital

Discussion

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Implication

Experimental study demonstrates that substituting domain III in CryIA(b) toxin enhances toxicity against Spodoptera exigua, indicating domain III drives receptor interaction and potency.

Key Points

To determine whether replacing domain III of the Bacillus thuringiensis CryIA(b) toxin with that of CryIC improves toxicity toward Spodoptera exigua and alters gut membrane recognition.
Generated cryIA(b)-cryIC hybrid genes using in vivo recombination and screened 120 recombinants to identify soluble protoxins.
Activated protoxins in vitro with trypsin to verify protease resistance and evaluated insecticidal activity via larval bioassays with Spodoptera exigua.
Characterized toxin-receptor interactions using biotinylated toxins and intact or solubilized brush border membrane vesicles from S. exigua midgut.
Screening identified two soluble hybrid protoxins containing domains I and II of CryIA(b) and domain III of CryIC, differing by only a single amino acid residue.
Hybrid protein H04 displayed substantially higher toxicity against S. exigua compared with parental CryIA(b) and demonstrated significantly greater potency than CryIC.
Domain III substitution abolished toxin binding to a 200-kDa membrane protein, whereas a reciprocal hybrid confirmed CryIA(b) domain III is required for this specific interaction.

Cite This Study

Maagd et al. (1996) studied this question.

synapsesocial.com/papers/6a6f2fa3660549caf2c3beb5 https://doi.org/10.1128/aem.62.5.1537-1543.1996

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Implication

Experimental study demonstrates that substituting domain III in CryIA(b) toxin enhances toxicity against Spodoptera exigua, indicating domain III drives receptor interaction and potency.

Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition

Discussion

Member takes

Implication

Key Points

Cite This Study

Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition

Discussion

Member takes

Implication

Key Points

Cite This Study

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