Bacillus thuringiensis: mechanism of action, resistance, and new applications: a review

No abstract is available for this paper.

• Publication year

  2016

• Venue

  Critical Reviews in Biotechnology

• Publication date

  2016-03-03

• Fields of study

  Agricultural and Food Sciences, Medicine, Biology, Environmental Science

• Identifiers
  DOI 10.3109/07388551.2014.960793PMID 25264571
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Pre-selecting resistance against individual Bti Cry toxins facilitates the development of resistance to the Bti toxins cocktail.

  2014cited by this paper
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• Solid-state cultivation of Bacillus thuringiensis R 176 with shrimp shells and rice straw as a substrate for chitinase production

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• Monitoring resistance to Bacillus thuringiensis subsp. israelensis in the field by performing bioassays with each Cry toxin separately

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• Utilization of silkworm litter and pupal waste-an eco-friendly approach for mass production of Bacillus thuringiensis.

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• Identification of a second cytotoxic protein produced by Bacillus thuringiensis A1470

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• Evaluation of two different culture media for the development of biopesticides based on Bacillus thuringiensis and their application in larvae of Aedes aegypti

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• Comparative binding of Cry1Ab and Cry1F Bacillus thuringiensis toxins to brush border membrane proteins from Ostrinia nubilalis, Ostrinia furnacalis and Diatraea saccharalis (Lepidoptera: Crambidae) midgut tissue.

  2013cited by this paper
• Alteration in Bacillus thuringiensis toxicity by curing gut flora: novel approach for mosquito resistance management

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• Current models of the mode of action of Bacillus thuringiensis insecticidal crystal proteins: a critical review.

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• Mutations in Domain I Interhelical Loops Affect the Rate of Pore Formation by the Bacillus thuringiensis Cry1Aa Toxin in Insect Midgut Brush Border Membrane Vesicles

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• A Novel Tenebrio molitor Cadherin Is a Functional Receptor for Bacillus thuringiensis Cry3Aa Toxin*

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• Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (Say)

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• Heliothis virescens and Manduca sextaLipid Rafts Are Involved in Cry1A Toxin Binding to the Midgut Epithelium and Subsequent Pore Formation*

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• Cry1A toxins of Bacillus thuringiensis bind specifically to a region adjacent to the membrane-proximal extracellular domain of BT-R(1) in Manduca sexta: involvement of a cadherin in the entomopathogenicity of Bacillus thuringiensis.

  2002cited by this paper
• Cadherin‐like receptor binding facilitates proteolytic cleavage of helix α‐1 in domain I and oligomer pre‐pore formation of Bacillus thuringiensis Cry1Ab toxin

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