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Bacillus thuringiensis toxins: an overview of their biocidal activity

Palma, Leopoldo, Muñoz, Delia, Berry, Colin, Murillo, Jesús and Caballero, Primitivo 2014. Bacillus thuringiensis toxins: an overview of their biocidal activity. Toxins 6 (12) , pp. 3296-3325. 10.3390/toxins6123296

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Abstract

Bacillus thuringiensis (Bt) is a Gram positive, spore-forming bacterium that synthesizes parasporal crystalline inclusions containing Cry and Cyt proteins, some of which are toxic against a wide range of insect orders, nematodes and human-cancer cells. These toxins have been successfully used as bioinsecticides against caterpillars, beetles, and flies, including mosquitoes and blackflies. Bt also synthesizes insecticidal proteins during the vegetative growth phase, which are subsequently secreted into the growth medium. These proteins are commonly known as vegetative insecticidal proteins (Vips) and hold insecticidal activity against lepidopteran, coleopteran and some homopteran pests. A less well characterized secretory protein with no amino acid similarity to Vip proteins has shown insecticidal activity against coleopteran pests and is termed Sip (secreted insecticidal protein). Bin-like and ETX_MTX2-family proteins (Pfam PF03318), which share amino acid similarities with mosquitocidal binary (Bin) and Mtx2 toxins, respectively, from Lysinibacillus sphaericus, are also produced by some Bt strains. In addition, vast numbers of Bt isolates naturally present in the soil and the phylloplane also synthesize crystal proteins whose biological activity is still unknown. In this review, we provide an updated overview of the known active Bt toxins to date and discuss their activities.

Item Type: Article
Date Type: Published Online
Status: Published
Schools: Biosciences
Subjects: Q Science > QR Microbiology
Uncontrolled Keywords: Bacillus thuringiensis; Bt biopesticides; toxic activity; Cry toxins; Cyt toxins; Vip toxins; Sip toxins; parasporins.
Publisher: Molecular Diversity Preservation International
ISSN: 2072-6651
Date of First Compliant Deposit: 30 March 2016
Date of Acceptance: 3 December 2014
Last Modified: 20 Feb 2019 16:43
URI: http://orca.cf.ac.uk/id/eprint/68552

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