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Article

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.

The Journal of biological chemistry - 20 Nov 2009

Pacheco Sabino, Gómez Isabel, Arenas Ivan, Saab-Rincon Gloria, Rodríguez-Almazán Claudia, Gill Sarjeet S, Bravo Alejandra, Soberón Mario

Abstract excerpt

Bacillus thuringiensis Cry toxins are used worldwide as insecticides in agriculture, in forestry, and in the control of disease transmission vectors. In the lepidopteran Manduca sexta, cadherin (Bt-R(1)) and aminopeptidase-N (APN) function as Cry1A toxin receptors. The interaction with Bt-R(1) pr...

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Identifiers

PMID: 19808680
DOI: 10.1074/jbc.M109.024968
PMCID: PMC2781692

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19808680-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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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.PMID 19808680Read ↗

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

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