Crystal structure of Cry51Aa1: A potential novel insecticidal aerolysin-type β-pore-forming toxin from Bacillus thuringiensis

Xu, Chang; Chinte, U.; Chen, Lirong; Yao, Qingqing; Meng, Ying; Zhou, Da‐Yong; Bi, Lijun; Rose, John P.; Adang, Michael J.; Wang, Bi-Cheng; Zhou, Yu; Sun, Ming

doi:10.1016/j.bbrc.2015.04.068

Cited by 32 publications

(36 citation statements)

References 29 publications

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“…This is expected, as native Cry51Aa1 and native Cry51Aa2 (TIC807), both of which have greater than 95% sequence identity with Cry51Aa2.834_16, also showed activity against L . decemlineata [25, 39]. However, no toxicity was observed toward larvae of a closely related species D .…”

Section: Discussionmentioning

confidence: 99%

“…The native Cry51Aa2 protein has been shown to share 97.7% sequence identity with the Cry51Aa1 protein described by Xu et al, [39] and both proteins are known to have activity against members of the Coleoptera [39]. Further, the native Cry51Aa2 protein was demonstrated to have activity at 500 ppm against two different hemipteran pest species, L .…”

Section: Introductionmentioning

confidence: 93%

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Characterization of the Activity Spectrum of MON 88702 and the Plant-Incorporated Protectant Cry51Aa2.834_16

et al. 2017

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The spectrum of insecticidal activity of Cry51Aa2.834_16 protein targeting hemipteran and thysanopteran insect pests in cotton was characterized by selecting and screening multiple pest and non-pest species, based on representation of ecological functional groups, taxonomic relatedness (e.g. relationship to species where activity was observed), and availability for effective testing. Seven invertebrate orders, comprising 12 families and 17 representative species were screened for susceptibility to Cry51Aa2.834_16 protein and/or the ability of the protein to protect against feeding damage in laboratory, controlled environments (e.g. greenhouse/growth chamber), and/or field studies when present in cotton plants. The screening results presented for Cry51Aa2.834_16 demonstrate selective and limited activity within three insect orders. Other than Orius insidiosus, no activity was observed for Cry51Aa2.834_16 against several groups of arthropods that perform key ecological roles in some agricultural ecosystems (e.g. pollinators, decomposers, and natural enemies).

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 93%

Characterization of the Activity Spectrum of MON 88702 and the Plant-Incorporated Protectant Cry51Aa2.834_16

et al. 2017

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“…Representatives of different structural classes of delta-endotoxins of B. thuringiensis are shown. Cry1Aa [PDB: 1CIY] [52] is a three-domain toxin; Cry6Aa is an alpha helical toxin (this work); Cry34 is an aegerolysin-like protein [PDB: 4JOX] [12] that acts as a binary toxin with Cry35, a Toxin_10 family protein [PDB: 4JP0] [12]; Cry51 is a member of the Etx/Mtx2 family [PDB: 4PKM] [11]; and Cyt1Aa, a member of the Bac_thur_toxin family [PDB: 3RON] [53]. All structures are to scale and colored according to secondary structure (alpha helix, red ; beta strands, yellow )…”

Section: Discussionmentioning

confidence: 99%

“…Some of these proteins share sequence homology to other known toxins; for example, Cry35 and Cry36 are related to the Bin and Cry49 toxins of Lysinibacillus sphaericus [6] and may share a proposed mechanism of action involving pore formation [7] and/or apoptosis [8]. The structures of the ß-sheet-rich toxins Cry45 (Parasporin4) [9], Cry46 (Parasporin 2) [10], and recently Cry51 [11] and the Cry34/Cry35 binary toxin [12] have been published but for many non-three-domain Cry proteins, neither structural data nor information on mechanism of action are available. One such Cry protein is Cry6Aa [13], a protein with activity against Coleoptera such as the Western Corn Rootworm Diabrotica virgifera virgifera [14] and a range of nematodes, including both free-living ( Caenorhabditis elegans and Panagrellus redivivus ) and plant pathogenic ( Heterodera glycines and Meloidogyne incognita ) species [15–18] that cause large-scale losses to agriculture [19].…”

Section: Introductionmentioning

confidence: 99%

The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins

Dementiev¹,

Board

Sitaram

et al. 2016

BMC Biol

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BackgroundThe Cry6 family of proteins from Bacillus thuringiensis represents a group of powerful toxins with great potential for use in the control of coleopteran insects and of nematode parasites of importance to agriculture. These proteins are unrelated to other insecticidal toxins at the level of their primary sequences and the structure and function of these proteins has been poorly studied to date. This has inhibited our understanding of these toxins and their mode of action, along with our ability to manipulate the proteins to alter their activity to our advantage. To increase our understanding of their mode of action and to facilitate further development of these proteins we have determined the structure of Cry6Aa in protoxin and trypsin-activated forms and demonstrated a pore-forming mechanism of action.ResultsThe two forms of the toxin were resolved to 2.7 Å and 2.0 Å respectively and showed very similar structures. Cry6Aa shows structural homology to a known class of pore-forming toxins including hemolysin E from Escherichia coli and two Bacillus cereus proteins: the hemolytic toxin HblB and the NheA component of the non-hemolytic toxin (pfam05791). Cry6Aa also shows atypical features compared to other members of this family, including internal repeat sequences and small loop regions within major alpha helices. Trypsin processing was found to result in the loss of some internal sequences while the C-terminal region remains disulfide-linked to the main core of the toxin. Based on the structural similarity of Cry6Aa to other toxins, the mechanism of action of the toxin was probed and its ability to form pores in vivo in Caenorhabditis elegans was demonstrated. A non-toxic mutant was also produced, consistent with the proposed pore-forming mode of action.ConclusionsCry6 proteins are members of the alpha helical pore-forming toxins – a structural class not previously recognized among the Cry toxins of B. thuringiensis and representing a new paradigm for nematocidal and insecticidal proteins. Elucidation of both the structure and the pore-forming mechanism of action of Cry6Aa now opens the way to more detailed analysis of toxin specificity and the development of new toxin variants with novel activities.Electronic supplementary materialThe online version of this article (doi:10.1186/s12915-016-0295-9) contains supplementary material, which is available to authorized users.

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“…Cry21 The structures of the insecticidal toxins BinB (PDB 3WA1 (Srisucharitpanit et al, 2014)), Cry35 (PDB 4JP0 (Kelker et al, 2014)), Cry23 (PDB 4RHZ), Cry45 (PDB 2D42 (Akiba et al, 2006)), Cry46 (PDB 2ZTB (Akiba et al, 2009)) and Cry51 (PDB 4PKM (Xu et al, 2015)) are…”

Section: Cry1mentioning

confidence: 99%

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

Berry

Crickmore

2017

Journal of Invertebrate Pathology

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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:

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Crystal structure of Cry51Aa1: A potential novel insecticidal aerolysin-type β-pore-forming toxin from Bacillus thuringiensis

Cited by 32 publications

References 29 publications

Characterization of the Activity Spectrum of MON 88702 and the Plant-Incorporated Protectant Cry51Aa2.834_16

Characterization of the Activity Spectrum of MON 88702 and the Plant-Incorporated Protectant Cry51Aa2.834_16

The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins

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

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