A Novel <i>Bacillus thuringiensis </i>(PS149B1) Containing a Cry34Ab1/Cry35Ab1 Binary Toxin Specific for the Western Corn Rootworm <i>Diabrotica virgifera virgifera</i> LeConte Forms Ion Channels in Lipid Membranes

Masson, Luke; Schwab, George; Mazza, Alberto; Brousseau, Roland; Potvin, L; Schwartz, Jean-Louis

doi:10.1021/bi048946z

Cited by 39 publications

(24 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As Cry6A, a nematicidal toxin shows low similarity to the three-domain Cry toxins and is lacking any of the five conserved blocks [32,164]. Cry22A and Cry34/Cry35 binary toxin have also been estimated with diverse structural characteristics [14,165,166]. As the number of discovered toxins rises, and novel structures are being solved, a new member of B. thuringiensis toxins would be described under these three categories or even according to other unidentified groups in the future.…”

Section: Discussionmentioning

confidence: 99%

Structural Insights into Bacillus thuringiensis Cry, Cyt and Parasporin Toxins

Wang

Zhou

et al. 2014

Toxins

143

112

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 99%

Structural Insights into Bacillus thuringiensis Cry, Cyt and Parasporin Toxins

Wang

Zhou

et al. 2014

Toxins

143

112

View full text Add to dashboard Cite

show abstract

“…Although the authors did not report results in their publication, Ellis et al (2002) indicated that mosquito screening assays of the type used to identify mosquitocidal L. sphaericus and B. thuringiensis strains did not identify a similar level of activity for the B. thuringiensis binary Cry34Ab1/Cry35Ab1 proteins. Moreover, Cry34Ab1 is the protein responsible for the majority of the insecticidal properties of maize 59122, and both proteins are needed to attain full membrane permeabilisation and insecticidal activity (Ellis et al, 2002;Masson et al, 2004). It is unlikely that Cry35Ab1 is active against dipterans, as the conditions in the gut of dipterans and coleopterans differ substantially (acidic in copleopterans and alkalic in dipterans).…”

mentioning

confidence: 99%

Scientific Opinion on an application from Pioneer Hi‐Bred International and Dow AgroSciences LLC (EFSA‐GMO‐NL‐2005‐23) for placing on the market of genetically modified maize 59122 for food and feed uses, import, processing and cultivation under Regulation (EC) No 1829/2003

2013

EFS2

View full text Add to dashboard Cite

This Scientific Opinion reports on a risk assessment on an application for placing on the market of genetically modified maize 59122 for import and processing for food and feed uses and cultivation. The EFSA GMO Panel considers that maize 59122 is unlikely to have any adverse effect on the environment, except for the possible evolution of resistance to the Cry34Ab1/Cry35Ab1 proteins in coleopteran target pests. The Panel recommends the implementation of appropriate and diversified insect resistance management strategies and case-specific monitoring to delay and monitor the possible evolution of resistance to Cry34Ab1/Cry35Ab1 in coleopteran target pests, respectively. In addition, the Panel recommends revision of the applicants' insect resistance management plan and the proposed post-market environmental monitoring plan. Although maize 59122 is tolerant to glufosinate-ammonium-based herbicides, the Panel did not assess the potential adverse effects associated with the use of such herbicides on maize 59122, as maize 59122 will not be marketed in the European Union as a herbicide-tolerant crop. This Scientific Opinion updates the previous Panel safety evaluation of the food and feed uses, and import and processing of maize 59122 and derived products. The Panel concludes that the information available for maize 59122 addresses the scientific comments raised by Member States and that maize 59122, as described in this application, is as safe as its conventional counterpart and commercial maize varieties with respect to potential adverse effects on human and animal health. If subjected to appropriate management measures, the cultivation of maize 59122 is unlikely to raise safety concerns for the environment.

show abstract

“…All of the other Toxin_10 proteins act with their specific partner proteins to form binary toxins as follows: BinA and BinB (both Toxin_10 proteins) (Broadwell et al, 1990;Oei et al, 1990); Cry34 (aegerolysin-like) and Cry35 (Toxin_10) (Kelker et al, 2014;Masson et al, 2004); Cry48 (3-domain) and Cry49 (Jones et al, 2007). The role of each protein in these binary pairs is clearly significant to understanding the specificity of the toxins and potential binding of both components presents further challenges to prediction.…”

Section: Sphaericus B Thuringiensis Bacillus Cereus and Paenibamentioning

confidence: 99%

Structural classification of insecticidal proteins – Towards an in silico characterisation of novel toxins

Berry

Crickmore

2017

Journal of Invertebrate Pathology

View full text Add to dashboard Cite

Article (Accepted Version) http://sro.sussex.ac.uk Berry, Colin and Crickmore, Neil (2017) Structural classification of insecticidal proteins -towards an in silico characterization of novel toxins. Journal of Invertebrate Pathology, 142. pp. 16-22. ISSN 0022-2011 This version is available from Sussex Research Online: http://sro.sussex.ac.uk/62164/ This document is made available in accordance with publisher policies and may differ from the published version or from the version of record. If you wish to cite this item you are advised to consult the publisher's version. Please see the URL above for details on accessing the published version. Copyright and reuse:Sussex Research Online is a digital repository of the research output of the University.Copyright and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable, the material made available in SRO has been checked for eligibility before being made available.Copies of full text items generally can be reproduced, displayed or performed and given to third parties in any format or medium for personal research or study, educational, or not-for-profit purposes without prior permission or charge, provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Accepted Manuscript Abstract:The increasing rate of discovery of new toxins with potential for the control of invertebrate pests through next generation sequencing, presents challenges for the identification of the best candidates for further development. A consideration of structural similarities between the different toxins suggest that they may be functionally less diverse than their low sequence similarities might predict. This is encouraging from the prospective of being able to use computational tools to predict toxin targets from their sequences, however more structure/function data are still required to reliably inform such predictions.Introduction:

show abstract

A Novel Bacillus thuringiensis (PS149B1) Containing a Cry34Ab1/Cry35Ab1 Binary Toxin Specific for the Western Corn Rootworm Diabrotica virgifera virgifera LeConte Forms Ion Channels in Lipid Membranes

Cited by 39 publications

References 42 publications

Structural Insights into Bacillus thuringiensis Cry, Cyt and Parasporin Toxins

Structural Insights into Bacillus thuringiensis Cry, Cyt and Parasporin Toxins

Scientific Opinion on an application from Pioneer Hi‐Bred International and Dow AgroSciences LLC (EFSA‐GMO‐NL‐2005‐23) for placing on the market of genetically modified maize 59122 for food and feed uses, import, processing and cultivation under Regulation (EC) No 1829/2003

Structural classification of insecticidal proteins – Towards an in silico characterisation of novel toxins

Contact Info

Product

Resources

About