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The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta.

Peptides - 1 Feb 2008

Jiménez-Juárez N, Muñoz-Garay C, Gómez I, Gill S S, Soberón M, Bravo A

Abstract excerpt

The insecticidal Cry toxins from Bacillus thuringiensis bacteria are pore-forming toxins that lyse midgut epithelial cells in insects. We have previously proposed that they form pre-pore oligomeric intermediates before membrane insertion. For formation of these oligomers coiled-coil structures are important, and helix alpha-3 from Cry toxins could form coiled-coils. Our data shows that different mutations in...

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Source

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Identifiers

PMID: 18226424
DOI: 10.1016/j.peptides.2007.09.026
PMCID: PMC2271039

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The pre-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta.PMID 18226424Read ↗

Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae.Semantic proximity Read ↗

Rearrangement of N-Terminal α-Helices of Bacillus thuringiensis Cry1Ab Toxin Essential for Oligomer Assembly and Toxicity.Semantic proximity Read ↗

Structural and functional studies of alpha-helix 5 region from Bacillus thuringiensis Cry1Ab delta-endotoxin.Semantic proximity Read ↗

The alpha-helix 4 residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins.Semantic proximity Read ↗

Evidence for intermolecular interaction as a necessary step for pore-formation activity and toxicity of Bacillus thuringiensis Cry1Ab toxin.Semantic proximity Read ↗

Dominant negative phenotype of Bacillus thuringiensis Cry1Ab, Cry11Aa and Cry4Ba mutants suggest hetero-oligomer formation among different Cry toxins.Semantic proximity Read ↗

Analysis of mutations in the pore-forming region essential for insecticidal activity of a Bacillus thuringiensis delta-endotoxin.Semantic proximity Read ↗

Domain II loop 3 of Bacillus thuringiensis Cry1Ab toxin is involved in a "ping pong" binding mechanism with Manduca sexta aminopeptidase-N and cadherin receptors.Semantic proximity Read ↗

Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection.Semantic proximity Read ↗

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Characterization of the mechanism of action of the genetically modified Cry1AbMod toxin that is active against Cry1Ab-resistant insects.Semantic proximity Read ↗

All domains of Cry1A toxins insert into insect brush border membranes.Semantic proximity Read ↗

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