ArticleScientific reports2018
Engineering Bacillus thuringiensis Cyt1Aa toxin specificity from dipteran to lepidopteran toxicity.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
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- Mutation of a Threonine Residue in αD-β4 Loop of Cyt2Aa2 Protein Influences Binding on Fluid Lipid Membranes.Toxins · 2023Article
- Insect chaperones Hsp70 and Hsp90 cooperatively enhance toxicity ofFrontiers in immunology · 2023Article
- Recombinant Mosquito Densovirus withToxins · 2022Article
- Role of Lectin in the Response ofFrontiers in immunology · 2022Review
- Can (We Make)Toxins · 2021Review
- Identification and recombinant expression of an antimicrobial peptide (cecropin B-like) from soybean pestThe journal of venomous animals and toxins including tropical diseases · 2021Article
- Bacillus thuringiensis Cry1Ab Domain III β-16 Is Involved in Binding to Prohibitin, Which Correlates with Toxicity against Helicoverpa armigera (Lepidoptera: Noctuidae).Applied and environmental microbiology · 2021Article
- In vivo nanoscale analysis of the dynamic synergistic interaction of Bacillus thuringiensis Cry11Aa and Cyt1Aa toxins in Aedes aegypti.PLoS pathogens · 2021Article
- Potential forToxins · 2020Review
- The Cytocidal Spectrum ofToxins · 2020Review
- FunctionalApplied and environmental microbiology · 2020Article
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- The C-terminal protoxin region ofThe Journal of biological chemistry · 2018Article
- "The Defined Toxin-binding Region of the Cadherin G-protein Coupled Receptor, BT-RJournal of proteomics & bioinformatics · 2018Article
- Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Cyt and Cry toxins are different pore-forming proteins produced by Bacillus thuringiensis bacteria, and used in insect-pests control. Cry-toxins have a complex mechanism involving interaction with several proteins in the insect gut such as aminopeptidase N (APN), alkaline phosphatase (ALP) and cadherin (CAD). It was shown that the loop regions of domain II of Cry toxins participate in receptor binding. Cyt-toxins are dipteran specific and interact with membrane lipids. We show that Cry1Ab domain II loop3 is involved in binding to APN, ALP and CAD receptors since point mutation Cry1Ab-G439D affected binding to these proteins. We hypothesized that construction of Cyt1A-hybrid proteins providing a binding site that recognizes gut proteins in lepidopteran larvae could result in improved Cyt1Aa toxin toward lepidopteran larvae. We constructed hybrid Cyt1Aa-loop3 proteins with increased binding interaction to Manduca sexta receptors and increased toxicity against two Lepidopteran pests, M. sexta and Plutella xylostella. The hybrid Cyt1Aa-loop3 proteins were severely affected in mosquitocidal activity and showed partial hemolytic activity but retained their capacity to synergize Cry11Aa toxicity against mosquitos. Our data show that insect specificity of Cyt1Aa toxin can be modified by introduction of loop regions from another non-related toxin with different insect specificity.
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