ReviewMicrobiology and molecular biology reviews : MMBR2007
Role of receptors in Bacillus thuringiensis crystal toxin activity.
Review in Microbiology and molecular biology reviews : MMBR, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 227 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
227 citing papers in PubMed, 677 citations in OpenAlex.
- RNAi: the next wave of green agriculture, challenges, and bridging the translational gap.Plant cell reports · 2026Review
- Biocontrol Potential of Native Entomopathogenic Bacteria AgainstPlants (Basel, Switzerland) · 2026Article
- A second locus associated with high-level resistance to Bt Cry1Ac inApplied and environmental microbiology · 2026Article
- The Entomotoxic Fungal LectinJournal of agricultural and food chemistry · 2026Article
- Gut plasma membrane proteomes of adults and larvae of the European honey bee, Apis mellifera.Scientific reports · 2025Article
- Structure Elucidation, Biological and Molecular Docking Studies of the δ‑Endotoxin Cry1Ca17 fromACS omega · 2025Article
- Characterization of Cry4Aa Toxin fromInsects · 2025Article
- Characterization of the spectrum of insecticidal activity of Cry1B.3, Cry1Da_7, and Vip3Cb1 proteins produced by lepidopteran-protected MON 89151 cotton.Scientific reports · 2025Article
- Ecological risk assessment for Cry1Da_7, Cry1B.3 and Vip3Cb1 proteins expressed in MON 89151 cotton: an insect-protected cotton with targeted activity against Lepidoptera.Transgenic research · 2025Article
- Cryo-EM identifies F-ENA of Bacillus thuringiensis as a widespread family of endospore appendages across Firmicutes.Nature communications · 2025Article
- An anti-idiotypic single domain antibody as Cry2Aa toxin mimotope and analysis of its binding region through molecular docking.BMC biotechnology · 2025Article
- Oligomer assembly ofToxicon: X · 2025Article
- Disruption of HaVipR1 confers Vip3Aa resistance in the moth crop pest Helicoverpa armigera.PLoS biology · 2025Article
- Interactions between insecticidal cry toxins and their receptors.Current genetics · 2025Review
- Potential Mechanisms Underlying the Minimal Impact of Cry1Ab1 Protein onInternational journal of molecular sciences · 2025Article
- Entomopathogenic Bacteria Species and Toxins Targeting Aphids (Hemiptera: Aphididae): A Review.Plants (Basel, Switzerland) · 2025Review
- Cryo-EM analysis of the Bacillus thuringiensis extrasporal matrix identifies F-ENA as a widespread family of endospore appendages across Firmicutes.Research square · 2025Article
- Cryo-EM analysis of thebioRxiv : the preprint server for biology · 2025Article
- Discovery and expression of insecticidal proteins via genome mining of novelFrontiers in microbiology · 2025Article
- Essential Role of Non-Conserved α4-HisProtein and peptide letters · 2025Article
167 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus thuringiensis produces crystalline protein inclusions with insecticidal or nematocidal properties. These crystal (Cry) proteins determine a particular strain's toxicity profile. Transgenic crops expressing one or more recombinant Cry toxins have become agriculturally important. Individual Cry toxins are usually toxic to only a few species within an order, and receptors on midgut epithelial cells have been shown to be critical determinants of Cry specificity. The best characterized of these receptors have been identified for lepidopterans, and two major receptor classes have emerged: the aminopeptidase N (APN) receptors and the cadherin-like receptors. Currently, 38 different APNs have been reported for 12 different lepidopterans. Each APN belongs to one of five groups that have unique structural features and Cry-binding properties. While 17 different APNs have been reported to bind to Cry toxins, only 2 have been shown to mediate toxin susceptibly in vivo. In contrast, several cadherin-like proteins bind to Cry toxins and confer toxin susceptibility in vitro, and disruption of the cadherin gene has been associated with toxin resistance. Nonetheless, only a small subset of the lepidopteran-specific Cry toxins has been shown to interact with cadherin-like proteins. This review analyzes the interactions between Cry toxins and their receptors, focusing on the identification and validation of receptors, the molecular basis for receptor recognition, the role of the receptor in resistant insects, and proposed models to explain the sequence of events at the cell surface by which receptor binding leads to cell death.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.