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Investigations of Bacillus thuringiensis Cry1 toxin receptor structure and function

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Entomopathogenic Bacteria: from Laboratory to Field Application

Abstract

Bacillus thuringiensis Cry1 proteins are highly toxic to some species of lepidopteran larvae. Cry proteins act on the brush border membrane through a multi-step process. The process includes Cry1 crystal solubilisation, activation by proteinases, attachment to receptors, then membrane insertion and permeation followed by cell lysis. Toxin binding to receptors is a pivotal event necessary for insect mortality. We review research that identified aminopeptidase N and cadherin-like proteins as Cry1 toxin receptors. Since enteric toxins recognise glycolipid receptors, we examined Manduca sexta brush border lipids as potential toxin receptors. M. sexta brush border membrane glycolipids lipids bound Cry1Ac toxin selectively on thin-layer chromatograph overlays. Because pore formation is necessary for toxicity, a functional receptor should catalyse Cry1-induced pore formation. Various data support aminopeptidases, cadherin-like proteins and glycolipids as “true” Cry1 receptors.

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  1. Affiliation Departments of Entomology, University of Georgia, Athens, Georgia, 30602, USA

    Stephen F. Garczynski & Michael J. Adang

  2. Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, 30602, USA

    Michael J. Adang

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  1. Institut Pasteur, Paris, France

    Jean-François Charles , Armelle Delécluse  & Christina Nielsen-Le Roux ,  & 

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Garczynski, S.F., Adang, M.J. (2000). Investigations of Bacillus thuringiensis Cry1 toxin receptor structure and function. In: Charles, JF., Delécluse, A., Roux, C.NL. (eds) Entomopathogenic Bacteria: from Laboratory to Field Application. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-1429-7_10

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