title: Structure, diversity, and evolution of protein toxins from spore-forming entomopathogenic bacteria.
abstract: Gram-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 diversity 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.
authors: Plant Research International B.V., 6700 AA Wageningen, Netherlands. ruud.demaagd@wur.nl
authors: Ruud A
authors: RA
authors: de Maagd
authors: Alejandra
authors: A
authors: Bravo
authors: Colin
authors: C
authors: Berry
authors: Neil
authors: N
authors: Crickmore
authors: H Ernest
authors: HE
authors: Schnepf
mesh_terms: D001407:Bacillus / Q000737:chemistry / Q000235:genetics; D001427:Bacterial Toxins / Q000737:chemistry* / Q000235:genetics; D005075:Biological Evolution; D016936:Gram-Positive Endospore-Forming Bacteria / Q000737:chemistry* / Q000235:genetics; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D001427:Bacterial Toxins; D011506:Proteins