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The Bacillus thuringiensis insecticidal toxin binds biotin-containing proteins

C Du1, K W Nickerson

  • 1School of Biological Sciences, University of Nebraska, Lincoln 68588-0666, USA.

Applied and Environmental Microbiology
|August 1, 1996
PubMed
Summary

Bacillus thuringiensis toxins bind to biotin-containing proteins in Manduca sexta larvae. This interaction, involving a specific motif in the toxin, suggests a novel mechanism for toxin recognition and inhibition of essential enzymes.

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Area of Science:

  • Insect biochemistry
  • Molecular toxicology
  • Microbial toxins

Background:

  • Brush border membrane vesicles (BBMVs) from Manduca sexta larvae contain proteins that bind streptavidin.
  • Bacillus thuringiensis (B. thuringiensis) toxins are known insecticidal proteins.

Purpose of the Study:

  • To investigate the interaction between B. thuringiensis toxins and proteins in M. sexta BBMVs.
  • To identify the nature of the binding and its functional implications.

Main Methods:

  • Biochemical assays using BBMVs, streptavidin-alkaline phosphatase conjugates, and biotin.
  • Toxin inhibition assays on pyruvate carboxylase activity.
  • Sequence analysis of conserved regions within the B. thuringiensis toxin.

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Main Results:

  • M. sexta BBMVs contain 85 and 120 kDa proteins that bind streptavidin.
  • Binding is inhibited by biotin and by an activated B. thuringiensis HD-73 toxin.
  • B. thuringiensis toxins bind to biotinylated proteins and inhibit pyruvate carboxylase activity.
  • A YAS biotin-specific motif in domain III of the toxin is implicated in biotin binding.

Conclusions:

  • B. thuringiensis toxins recognize and bind to biotin-containing proteins in M. sexta.
  • This interaction may represent a novel mechanism of toxin action or detoxification.
  • The 120 kDa protein is distinct from known Cry1Ac toxin receptors.