Interaction of Bacillus thuringiensis svar. israelensis Cry toxins with binding sites from Aedes aegypti (Diptera: Culicidae) larvae midgut

FEMS Microbiol Lett. 2007 Jan;266(2):163-9. doi: 10.1111/j.1574-6968.2006.00527.x. Epub 2006 Nov 21.

Abstract

This work shows in vitro processing of Bacillus thuringiensis svar. isralensis Cry toxins and the capacity of the active fragments to bind the midgut microvilli of Aedes aegypti larvae. Processing of Cry11Aa, Cry4Aa and Cry4Ba yielded double fragments of 38-30, 45-20 and 45-18 kDa, respectively. Competition assays showed that all active (125)I-Cry toxins are able to specifically bind to brush border membrane fractions and they might share a common class of binding sites. The values of IC(50) suggested that toxins do not display high affinity for the receptors from brush border membrane fractions, while dissociation assays showed that binding was irreversible, indicating the insertion of toxins in the cell membrane.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Bacterial Proteins / pharmacology
  • Bacterial Toxins / chemistry
  • Bacterial Toxins / metabolism*
  • Bacterial Toxins / pharmacology
  • Binding Sites
  • Binding, Competitive
  • Cell Membrane / metabolism
  • Culicidae / metabolism*
  • Endotoxins / chemistry
  • Endotoxins / metabolism*
  • Endotoxins / pharmacology
  • Gastrointestinal Tract / metabolism
  • Hemolysin Proteins / chemistry
  • Hemolysin Proteins / metabolism*
  • Hemolysin Proteins / pharmacology
  • Inhibitory Concentration 50
  • Larva / drug effects
  • Larva / growth & development
  • Larva / metabolism
  • Microvilli / metabolism
  • Molecular Weight
  • Protein Binding
  • Radioligand Assay

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Bacterial Toxins
  • Endotoxins
  • Hemolysin Proteins
  • insecticidal crystal protein, Bacillus Thuringiensis