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Review
. 2025 Mar 29;71(1):9.
doi: 10.1007/s00294-025-01312-1.

Interactions between insecticidal cry toxins and their receptors

Affiliations
Review

Interactions between insecticidal cry toxins and their receptors

Pravukalyan Mohanty et al. Curr Genet. .

Abstract

Bacillus thuringiensis is a prominent, eco-friendly entomopathogenic bacterium used as a plant-incorporated toxin in genetically modified crops and as a stomach poison for insects in the form of spore formulations. Upon entering the alkaline environment of the insect gut, the toxin undergoes proteolytic breakdown, converting the protoxin into its activated form. The activated toxin then binds to receptors, forming pores that disrupt the ionic balance within the cell, ultimately leading to the insect's death. Alongside the four major receptors (Cadherin, ABCC, APN, and ALP), several other notable receptors are present on the Brush Border Membrane Vesicle of insects. Binding to these receptors plays a crucial role, and any mutations in these receptors can result in improper binding, leading to the development of resistant insect strains. This review explores the major receptors of insecticidal Cry toxins, the intricate interactions between toxins and receptors, receptor mutations, and strategies to overcome the resistance.

Keywords: Bacillus thuringiensis; Binding; Cry toxins; Mutation; Pest management; Receptors.

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Conflict of interest statement

Declarations. Ethics approval and consent to participate: Not applicable. Consent for publication: Not applicable. Competing interests: The authors declare no competing interests.

References

    1. Abdullah MAF, Valaitis AP, Dean DH (2006) Identification of a Bacillus Thuringiensis Cry11Ba toxin-binding aminopeptidase from the mosquito, Anopheles quadrimaculatus. BMC Biochem 7:16. https://doi.org/10.1186/1471-2091-7-16 - DOI - PubMed - PMC
    1. Abdullah MAF, Moussa S, Taylor MD, Adang MJ (2009) Manduca sexta (Lepidoptera: Sphingidae) Cadherin fragments function as synergists for Cry1A and Cry1C Bacillus Thuringiensis toxins against noctuid moths Helicoverpa Zea, agrotis ipsilon and Spodoptera Exigua. Pest Manag Sci 65:1097–1103. https://doi.org/10.1002/ps.1798 - DOI - PubMed
    1. Adang MJ (2004) Insect aminopeptidase N. Handbook of proteolytic enzymes. Elsevier, pp 296–299
    1. Adegawa S, Wang Y, Waizumi R, Iizuka T, Takasu Y, Watanabe K, Sato R (2024) Cry toxins use multiple ATP-Binding cassette transporter subfamily C members as Low-Efficiency receptors in Bombyx Mori. Biomolecules 14(3):271. https://doi.org/10.3390/biom14030271 - DOI - PubMed - PMC
    1. Aimanova KG, Zhuang M, Gill SS (2006) Expression of Cry1Ac Cadherin receptors in insect midgut and cell lines. J Invertebr Pathol 92:178–187. https://doi.org/10.1016/j.jip.2006.04.011 - DOI - PubMed

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