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Insecticidal toxins from Photorhabdus bacteria and their potential use in agriculture


Reference:

Ffrench-Constant, R. H., Dowling, A. and Waterfield, N. R., 2007. Insecticidal toxins from Photorhabdus bacteria and their potential use in agriculture. Toxicon, 49 (4), pp. 436-451.

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Official URL:

http://dx.doi.org/10.1016/j.toxicon.2006.11.019

Abstract

Most of the insecticidal toxins used in agriculture come from a single bacterium Bacillus thuringiensis or 'Bt'. Here we review our work on the array of toxins produced by Photorhabdus and Xenorhabdus bacteria that are symbiotic with entomopathogenic nematodes, and discuss their potential for use in agriculture as alternatives to Bt. Despite the fact that both Photorhabdus and Xenorhabdus are introduced directly into the insect blood stream by their nematode vectors, they produce a range of toxins with both oral and injectable insecticidal activity. The toxin complexes (Tc's) are large orally active toxins that are displayed on the outer surface of the bacterium. They require three components (A-C) for full toxicity and one 'A' component has been successfully expressed in transgenic Arabidopsis to confer insect resistance. One such group of Tc's, the PirAB binary toxins, have oral activity against mosquitoes and some caterpillar pests. Their mode of action is not known but they show significant sequence similarity to a recently described neurotoxin beta-leptinotarsin-h isolated from the blood of the Colorado potato beetle. Other toxins such as 'makes caterpillars floppy' (Mcf) and proteins encoded by the 'Photorhabdus virulence cassettes' (PVCs) only show injectable activity. Mcf1 promotes apoptosis in a wide range of cells and appears to mimic mammalian BH3 domain-only proteins in the mitochondrion whereas the mode of action of the PVCs remains undetermined. The likely biological reasons for the massive functional redundancy in Pholorhabdus insecticidal toxins are discussed.

Details

Item Type Articles
CreatorsFfrench-Constant, R. H., Dowling, A. and Waterfield, N. R.
DOI10.1016/j.toxicon.2006.11.019
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code3562

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