Structural Insights into Bacillus thuringiensis Cry, Cyt and Parasporin Toxins

Toxins

Chengchen Xu²  Bi-Cheng Wang¹  Ziniu Yu² 

[1] Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA; E-Mail:;State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; E-Mail:

关键词: Bacillus thuringiensis;    Cry toxin;    Cyt toxin;    parasporin;    pore-forming toxins;   

DOI  :  10.3390/toxins6092732

来源: mdpi

【 摘 要 】

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 α-PFTs, Cyt toxin type β-PFTs and aerolysin type β-PFTs. Structures from each group are elucidated and discussed in relation to the latest data, respectively.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.