How Bacillus thuringiensis has evolved specific toxins to colonize the insect world.

By R. A. Maagd, A. Bravo, Neil Crickmore. Trends in Genetics, 2001

693 citations recorded by the source corpus.

Bacillus thuringiensis is a bacterium of great agronomic and scientific interest. Together the subspecies of this bacterium colonize and kill a large variety of host insects and even nematodes, but each strain does so with a high degree of specificity. This is mainly determined by the arsenal of crystal proteins that the bacterium produces during sporulation. Here we describe the properties of these toxin proteins and the current knowledge of the basis for their specificity. Assessment of phylogenetic relationships of the three domains of the active toxin and experimental results indicate how sequence divergence in combination with domain swapping by homologous recombination might have caused this extensive range of specificities.

Subfields: Insect Science, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/51882943243588950bdfddc08bbda1b24520612c

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Insect Science

1. M. Soberón
2. Angelika Hilbeck
3. Jörg E. U. Schmidt

In Molecular Biology

1. M. Soberón
2. Liliana Pardo-López
3. A. Bravo
4. Angelika Hilbeck
5. Jörg E. U. Schmidt
6. X. Hong

Citations in the corpus

• Another View on Bt Proteins - How Specific are They and What Else Might They Do? (2006, background): “Despite considerable research and literature about Bt, the evolutionary role of the toxins still remains subject of discussion (de Maagd et al., 2001).”
• Role of Receptors in Bacillus thuringiensis Crystal Toxin Activity (2007, background): “amplification, leading to the evolution of new toxins (29).”
• Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for insect control. (2007, background): “An analysis of the phylogenetic relationships of the isolated domains of members of the threedomain Cry family revealed interesting features regarding the creation of diversity in this protein family (Bravo, 1997; de Maagd et al., 2001).”
• Progress in research on acute hepatopancreatic necrosis disease (AHPND) (2016, background): “Gut microflora can then enter the hemocoel of the larva and propagate (de Maagd et al. 2001; Bravo et al. 2007).”
• Expression of Cry5B protein from Bacillus thuringiensis in plant roots confers resistance to root-knot nematode (2008, background): “proteins used in transgenic crops, e.g., Cry1Aab ( de Maagd et al., 2001; Marroquin et al., 2000; Schnepf et al., 1998).”
• Bacillus thuringiensis insecticidal three-domain Cry toxins: mode of action, insect resistance and consequences for crop protection. (2013, background): “The main difference between the 65- and 130-kDa 3d-Cry toxin is the C-terminal extension that is found in the 130-kDa protoxins and is dispensable for toxicity, as it is cleaved by proteases present in the larval midgut (de Maagd et al., 2001).”
• Bacillus thuringiensis and its pesticidal crystal proteins (2020, background): “Thermal treatment of spores, often with enrichment or antibiotic selection, usually requires insulation ([12]).”
• Bacillus thuringiensis: A story of a successful bioinsecticide. (2011, background): “Phylogenetic analysis of the 3D-Cry toxin family revealed that Cry toxin variability evolved by two main processes; the independent evolution of the three functional domains and by domain III swapping among different toxins (Bravo, 1997; de Maagd et al., 2001).”
• Bacillus thuringiensis Toxins: An Overview of Their Biocidal Activity (2014, neutral): “(III), galactose-binding domain, involved in receptor binding and pore formation [7,21,38,39].”