Publications by authors named "Y Bel"
Article Synopsis
- The increased focus on biological pesticides for crop protection has led to studying Bacillus thuringiensis (Bt) and its toxic proteins against harmful root-knot nematodes.
- In laboratory tests, proteins Cry5, Cry21, App6, and Xpp55 showed high levels of toxicity against root-knot nematodes M. incognita and M. javanica.
- However, in field tests with cucumber and tomato plants, the effectiveness of the Bt proteins varied by plant type, suggesting that how these proteins are delivered is critical for their pest control success.
Draft genome sequence of strain V-AB8.18, a novel isolate with potential nematicidal activity.
Microbiol Resour Announc
July 2024
We report the draft genome of strain V-AB8.18, comprising 308 contigs totaling 6,182,614 bp, with 35% G + C content. It contains 6,151 putative protein-coding genes, including App6 and Cry5-like crystal proteins, exhibiting 99% pairwise identity to nematicidal proteins App6Aa2 and Cry5Ba2, active against and .
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- Nanotechnology is used to enhance the stability of Bacillus thuringiensis (Bt) proteins in harsh environmental conditions, particularly through the creation of Pickering emulsions.
- The use of pH-sensitive polymers in these emulsions allows for the targeted release of the Cry1Ab protein in the alkaline gut of lepidopteran pests, improving its effectiveness as an insecticide.
- Tests showed that encapsulating Cry1Ab with Cu-SQDs/S-CN and GO nanomaterials significantly protected it from degradation due to UV light and heat, leading to increased residual activity and reduced degradation rates.
Bacillus thuringiensis (Bt) is a Gram-positive bacterium that accumulates pesticidal proteins (Cry and Cyt) in parasporal crystals. Proteins from the Cry5, App6 (formerly Cry6), Cry12, Cry13, Cry14, Cry21, and Xpp55 (formerly Cry55) families have been identified as toxic to nematodes. In this study, a total of 846 Bt strains belonging to four collections were analyzed to determine the diversity and distribution of the Bt Cry nematicidal protein genes.
View Article and Find Full Text PDFVip3 proteins are produced by Bacillus thuringiensis and are toxic against lepidopterans, reason why the vip3Aa gene has been introduced into cotton and corn to control agricultural pests. Recently, the structure of Vip3 proteins has been determined and consists of a tetramer where each monomer is composed of five structural domains. The transition from protoxin to the trypsin-activated form involves a major conformational change of the N-terminal Domain I, which is remodelled into a tetrameric coiled-coil structure that is thought to insert into the apical membrane of the midgut cells.
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