Journal
TOXINS
Volume 6, Issue 9, Pages 2732-2770Publisher
MDPI
DOI: 10.3390/toxins6092732
Keywords
Bacillus thuringiensis; Cry toxin; Cyt toxin; parasporin; pore-forming toxins
Categories
Funding
- National Basic Research Program of China (973 Program) [2013CB127504]
- State Key Program of National Natural Science of China [30930004]
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Since the first X-ray structure of Cry3Aa was revealed in 1991, numerous structures of B. thuringiensis toxins have been determined and published. In recent years, functional studies on the mode of action and resistance mechanism have been proposed, which notably promoted the developments of biological insecticides and insect-resistant transgenic crops. With the exploration of known pore-forming toxins (PFTs) structures, similarities between PFTs and B. thuringiensis toxins have provided great insights into receptor binding interactions and conformational changes from water-soluble to membrane pore-forming state of B. thuringiensis toxins. This review mainly focuses on the latest discoveries of the toxin working mechanism, with the emphasis on structural related progress. Based on the structural features, B. thuringiensis Cry, Cyt and parasporin toxins could be divided into three categories: three-domain type alpha-PFTs, Cyt toxin type beta-PFTs and aerolysin type beta-PFTs. Structures from each group are elucidated and discussed in relation to the latest data, respectively.
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