Structure, diversity and evolution of protein toxins from spore-forming entomopathogenic bacteria

R.A. de Maagd, A. Bravo, C. Berry, N. Crickmore, H.E. Schnepf

    Research output: Contribution to journalArticleAcademicpeer-review

    293 Citations (Scopus)

    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
    Original languageEnglish
    Pages (from-to)409-433
    JournalAnnual Review of Genetics
    Volume37
    DOIs
    Publication statusPublished - 2003

    Keywords

    • sphaericus binary toxin
    • thuringiensis subsp israelensis
    • brush-border membranes
    • vegetative insecticidal protein
    • pesticidal crystal proteins
    • culex-pipiens diptera
    • bacillus-thuringiensis
    • delta-endotoxin
    • mosquitocidal toxin
    • domain-iii

    Fingerprint

    Dive into the research topics of 'Structure, diversity and evolution of protein toxins from spore-forming entomopathogenic bacteria'. Together they form a unique fingerprint.

    Cite this