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Structure, diversity, and evolution of protein toxins from spore-forming entomopathogenic bacteria
journal contribution
posted on 2023-06-08, 09:55 authored by Ruud A de Maagd, Alejandra Bravo, Colin Berry, Neil CrickmoreNeil Crickmore, H Ernest SchnepfGram-positive spore-forming entomopathogenic bacteria can utilize a large variety of protein toxins to help them invade, infect, and finally kill their hosts, through their action on the insect midgut. These toxins belong to a number of homology groups containing a diversify of protein structures and modes of Action. In many cases; the toxins consist of unique folds or novel combinations of domains having known protein folds. Some of the toxins display a similar structure and mode of action to-certain toxins of mammalian pathogens" suggesting a common evolutionary origin. Most of these toxins are produced in large amounts during sporulation and have the remarkable feature that they are localized in parasporal crystals. Localization of multiple toxin-encoding genes on plasmids together with mobilizable elements enables bacteria to shuffle their armory of toxins. Recombination between, toxin genes and sequence divergence has resulted in a wide range of host specificities.
History
Publication status
- Published
Journal
Annual Review of GeneticsISSN
0066-4197Volume
37Page range
409-433Pages
25.0Department affiliated with
- Biochemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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