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Characterization of cry Genes in a Mexican Bacillus thuringiensis Strain Collection
- A. Bravo, Sergio Sarabia, R. Quintero
- Medicine, BiologyApplied and Environmental Microbiology
- 1 December 1998
The results indicate the presence of strains that may harbor potentially novel Cry proteins as well as strains with combinations of less frequently observed cry genes, which could lead to novel bioinsecticidal products.
Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect control.
Bacillus thuringiensis: A story of a successful bioinsecticide.
RNA interference in Lepidoptera: an overview of successful and unsuccessful studies and implications for experimental design.
Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains.
How Bacillus thuringiensis has evolved specific toxins to colonize the insect world.
Structure, diversity, and evolution of protein toxins from spore-forming entomopathogenic bacteria.
- R. D. de Maagd, A. Bravo, C. Berry, N. Crickmore, H. E. Schnepf
- BiologyAnnual review of genetics
- 28 November 2003
Most of the toxins used by Gram-positive spore-forming entomopathogenic bacteria are produced in large amounts during sporulation and have the remarkable feature that they are localized in parasporal crystals.
Cadherin‐like receptor binding facilitates proteolytic cleavage of helix α‐1 in domain I and oligomer pre‐pore formation of Bacillus thuringiensis Cry1Ab toxin
Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection.
Activity of Cry1AMod toxins, which are able to form toxin oligomers in the absence of receptors, against different resistant populations, supports the hypothesis that toxin oligomerization is a limiting step in the Cry insecticidal activity.
Bacillus thuringiensis subsp. israelensis Cyt1Aa synergizes Cry11Aa toxin by functioning as a membrane-bound receptor.
- C. Perez, L. E. Fernández, A. Bravo
- BiologyProceedings of the National Academy of Sciences…
- 20 December 2005
Evidence is provided that Cyt1Aa functions as a receptor of Cry11Aa, a highly effective pathogenic bacterium that produces a toxin and also its functional receptor, promoting toxin binding to the target membrane and causing toxicity.