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      Structural Insights into Bacillus thuringiensis Cry, Cyt and Parasporin Toxins

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          Abstract

          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.

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          ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins.

          Patrice Gouet, Xavier Robert, Emmanuel Courcelle (2003)
          The fortran program ESPript was created in 1993, to display on a PostScript figure multiple sequence alignments adorned with secondary structure elements. A web server was made available in 1999 and ESPript has been linked to three major web tools: ProDom which identifies protein domains, PredictProtein which predicts secondary structure elements and NPS@ which runs sequence alignment programs. A web server named ENDscript was created in 2002 to facilitate the generation of ESPript figures containing a large amount of information. ENDscript uses programs such as BLAST, Clustal and PHYLODENDRON to work on protein sequences and such as DSSP, CNS and MOLSCRIPT to work on protein coordinates. It enables the creation, from a single Protein Data Bank identifier, of a multiple sequence alignment figure adorned with secondary structure elements of each sequence of known 3D structure. Similar 3D structures are superimposed in turn with the program PROFIT and a final figure is drawn with BOBSCRIPT, which shows sequence and structure conservation along the Calpha trace of the query. ESPript and ENDscript are available at http://genopole.toulouse.inra.fr/ESPript.
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            Bacillus thuringiensis and its pesticidal crystal proteins.

            E Schnepf, N Crickmore, J Van Rie … (1998)
            During the past decade the pesticidal bacterium Bacillus thuringiensis has been the subject of intensive research. These efforts have yielded considerable data about the complex relationships between the structure, mechanism of action, and genetics of the organism's pesticidal crystal proteins, and a coherent picture of these relationships is beginning to emerge. Other studies have focused on the ecological role of the B. thuringiensis crystal proteins, their performance in agricultural and other natural settings, and the evolution of resistance mechanisms in target pests. Armed with this knowledge base and with the tools of modern biotechnology, researchers are now reporting promising results in engineering more-useful toxins and formulations, in creating transgenic plants that express pesticidal activity, and in constructing integrated management strategies to insure that these products are utilized with maximum efficiency and benefit.
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              Bacillus thuringiensis: A story of a successful bioinsecticide.

              Alejandra Bravo, Supaporn Likitvivatanavong, Sarjeet Gill … (2011)
              Bacillus thuringiensis (Bt) bacteria are insect pathogens that rely on insecticidal pore forming proteins known as Cry and Cyt toxins to kill their insect larval hosts. At least four different non-structurally related families of proteins form the Cry toxin group of toxins. The expression of certain Cry toxins in transgenic crops has contributed to an efficient control of insect pests resulting in a significant reduction in chemical insecticide use. The mode of action of the three domain Cry toxin family involves sequential interaction of these toxins with several insect midgut proteins facilitating the formation of a pre-pore oligomer structure and subsequent membrane insertion that leads to the killing of midgut insect cells by osmotic shock. In this manuscript we review recent progress in understanding the mode of action of this family of proteins in lepidopteran, dipteran and coleopteran insects. Interestingly, similar Cry-binding proteins have been identified in the three insect orders, as cadherin, aminopeptidase-N and alkaline phosphatase suggesting a conserved mode of action. Also, recent data on insect responses to Cry toxin attack is discussed. Finally, we review the different Bt based products, including transgenic crops, that are currently used in agriculture. Copyright © 2011 Elsevier Ltd. All rights reserved.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Toxins (Basel)
                Journal ID (iso-abbrev): Toxins (Basel)
                Journal ID (publisher-id): toxins
                Title: Toxins
                Publisher: MDPI
                ISSN (Electronic): 2072-6651
                Publication date (Electronic): 16 September 2014
                Publication date Collection: September 2014
                Volume: 6
                Issue: 9
                Pages: 2732-2770
                Affiliations
                [1 ]State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; E-Mail: chenchen.609609@ 123456gmail.com
                [2 ]Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA; E-Mail: wang@ 123456bcl1.bmb.uga.edu
                Author notes
                [* ]Authors to whom correspondence should be addressed; E-Mails: yz41@ 123456mail.hzau.edu.cn (Z.Y.); m98sun@ 123456mail.hzau.edu.cn (M.S.); Tel.: +86-27-8739-6030 (Z.Y.); +86-27-8728-3455 (M.S.); Fax: +86-27-8728-7254 (Z.Y.); +86-27-8728-0670 (M.S.).
                Article
                Publisher ID: toxins-06-02732
                DOI: 10.3390/toxins6092732
                PMC ID: 4179158
                PubMed ID: 25229189
                SO-VID: 67922c8e-9687-42cc-a792-6630a8a728c9
                Copyright © © 2014 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 29 April 2014
                Date revision received : 26 August 2014
                Date accepted : 28 August 2014
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular medicine
                Keywords: bacillus thuringiensis,cry toxin,cyt toxin,parasporin,pore-forming toxins
                Data availability:
                ScienceOpen disciplines: Molecular medicine
                Keywords: bacillus thuringiensis, cry toxin, cyt toxin, parasporin, pore-forming toxins

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