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Book: Bt resistance

Soberón, Mario

characterization and strategies for GM crops producing Bacillus thuringiensis toxins

(CABI biotechnology series ; 4)

2015

Author's details	ed. by Mario Soberón
Series title	CABI biotechnology series ; 4
Collection
Keywords	Transgenic plants/Insect resistance ; Bacillus thuringiensis
Subject code	632.8
Language	English
Size	XII, 213 S. : graph. Darst., Kt., 25 cm
Publisher	CABI
Publishing place	Wallingford u.a.
Publishing country	Great Britain
Document type	Book
Note	Formerly CIP. ; Includes bibliographical references and index
HBZ-ID	HT018948366
ISBN	978-1-78064-437-0 ; 1-78064-437-X
Database	Catalogue ZB MED Nutrition, Environment, Agriculture

In stock of ZB MED Bonn / Germany

Shelf mark	Loan status	Location
164/122	available for loan (reading room)	Freihandmagazin (U1)

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Article ; Online: Can microbial-based insecticides replace chemical pesticides in agricultural production?

Bravo, Alejandra / Soberón, Mario

Microbial biotechnology

2023 Volume 16, Issue 11, Page(s) 2011–2014

Abstract: Extensive use of chemical insecticides to control insect pests in agriculture has improved yields and production of high-quality food products. However, chemical insecticides have been shown to be harmful also to beneficial insects and many other ... ...

Abstract	Extensive use of chemical insecticides to control insect pests in agriculture has improved yields and production of high-quality food products. However, chemical insecticides have been shown to be harmful also to beneficial insects and many other organisms like vertebrates. Thus, there is a need to replace those chemical insecticides by other control methods in order to protect the environment. Insect pest pathogens, like bacteria, viruses or fungi, are interesting alternatives for production of microbial-based insecticides to replace the use of chemical products in agriculture. Organic farming, which does not use chemical pesticides for pest control, relies on integrated pest management techniques and in the use of microbial-based insecticides for pest control. Microbial-based insecticides require precise formulation and extensive monitoring of insect pests, since they are highly specific for certain insect pests and in general are more effective for larval young instars. Here, we analyse the possibility of using microbial-based insecticides to replace chemical pesticides in agricultural production.
MeSH term(s)	Animals ; Insecticides ; Pesticides ; Pest Control, Biological/methods ; Agriculture/methods ; Insecta/microbiology
Chemical Substances	Insecticides ; Pesticides
Language	English
Publishing date	2023-07-18
Publishing country	United States
Document type	Editorial
ZDB-ID	2406063-X
ISSN	1751-7915 ; 1751-7915
ISSN (online)	1751-7915
ISSN	1751-7915
DOI	10.1111/1751-7915.14316
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Mining versus in vitro evolution for the selection of novel microbial insecticidal proteins.

Bravo, Alejandra / Soberón, Mario

Microbial biotechnology

2022 Volume 15, Issue 10, Page(s) 2518–2520

MeSH term(s)	Endotoxins ; Insecticides/pharmacology ; Mining
Chemical Substances	Endotoxins ; Insecticides
Language	English
Publishing date	2022-08-24
Publishing country	United States
Document type	Journal Article
ZDB-ID	2406063-X
ISSN	1751-7915 ; 1751-7915
ISSN (online)	1751-7915
ISSN	1751-7915
DOI	10.1111/1751-7915.14136
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Article ; Online: A major conformational change of N-terminal helices of Bacillus thuringiensis Cry1Ab insecticidal protein is necessary for membrane insertion and toxicity.

Pacheco, Sabino / Gómez, Isabel / Soberón, Mario / Bravo, Alejandra

The FEBS journal

2023 Volume 290, Issue 10, Page(s) 2692–2705

Abstract: Pore forming toxins rely on oligomerization for membrane insertion to kill their targets. Bacillus thuringiensis produces insecticidal Cry-proteins composed of three domains that form pores that kill the insect larvae. Domain I is involved in ... ...

Abstract	Pore forming toxins rely on oligomerization for membrane insertion to kill their targets. Bacillus thuringiensis produces insecticidal Cry-proteins composed of three domains that form pores that kill the insect larvae. Domain I is involved in oligomerization and membrane insertion, whereas Domains II and III participate in receptor binding and specificity. However, the structural changes involved in membrane insertion of these proteins remain unsolved. The most widely accepted model for membrane insertion, the 'umbrella model', proposed that the α-4/α-5 hairpin of Domain I swings away and is inserted into the membrane. To determine the topology of Cry1Ab in the membrane, disulfide bonds linking α-helices of Domain I were introduced to restrict their movement. Disulfide bonds between helices α-2/α-3 or α-3/α-4 lost oligomerization and toxicity, indicating that movement of these helices is needed for insecticidal activity. By contrast, disulfide bonds linking helices α-5/α-6 did not affect toxicity, which contradicts the 'umbrella model'. Additionally, Föster resonance energy transfer closest approach analyses measuring distances of different points in the toxin to the membrane plane and collisional quenching assays analysing the protection of specific fluorescent-labeled residues to the soluble potassium iodide quencher in the membrane inserted state were performed. Overall, the data show that Domain I from Cry1Ab may undergo a major conformational change during its membrane insertion, where the N-terminal region (helices α-1 to α-4) participates in oligomerization and toxicity, probably forming an extended helix. These data break a paradigm, showing a new 'folding white-cane model', which better explains the structural changes of Cry toxins during insertion into the membrane.
MeSH term(s)	Animals ; Insecticides/toxicity ; Bacillus thuringiensis/genetics ; Bacillus thuringiensis/chemistry ; Bacillus thuringiensis/metabolism ; Bacterial Proteins/metabolism ; Endotoxins/chemistry ; Hemolysin Proteins/metabolism ; Disulfides/metabolism ; Larva/metabolism
Chemical Substances	insecticidal crystal protein, Bacillus Thuringiensis ; Insecticides ; Bacterial Proteins ; Endotoxins ; Hemolysin Proteins ; Disulfides
Language	English
Publishing date	2023-01-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.16710
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Performance insights into spray-dryer microencapsulated Bacillus thuringiensis cry pesticidal proteins with gum arabic and maltodextrin for effective pest control.

de Oliveira, Jhones Luiz / Gómez, Isabel / Sánchez, Jorge / Soberón, Mario / Polanczyk, Ricardo Antonio / Bravo, Alejandra

Applied microbiology and biotechnology

2024 Volume 108, Issue 1, Page(s) 181

Abstract: Bacillus thuringiensis (Bt) produces crystals composed mainly of Cry pesticidal proteins with insecticidal activity against pests but are highly susceptible to degradation by abiotic factors. In this sense, encapsulation techniques are designed to ... ...

Abstract	Bacillus thuringiensis (Bt) produces crystals composed mainly of Cry pesticidal proteins with insecticidal activity against pests but are highly susceptible to degradation by abiotic factors. In this sense, encapsulation techniques are designed to improve their performance and lifetime. However, the effects of polymeric matrix encapsulation such as gum arabic and maltodextrin by spray-dryer in the mechanisms of action of Bt kurstaki and Bt aizawai are unknown. We analyzed crystal solubilization, protoxin activation, and receptor binding after microencapsulation and compared them with commercial non-encapsulated products. Microencapsulation did not alter protein crystal solubilization, providing 130 kDa (Cry1 protoxin) and 70 kDa (Cry2 protoxin). Activation with trypsin, chymotrypsin, and larval midgut juice was analyzed, showing that this step is highly efficient, and the protoxins were cleaved producing similar ~ 55 to 65 kDa activated proteins for both formulations. Binding assays with brush border membrane vesicles of Manduca sexta and Spodoptera frugiperda larvae provided a similar binding for both formulations. LC
MeSH term(s)	Animals ; Pesticides/pharmacology ; Gum Arabic ; Bacillus thuringiensis ; Biological Control Agents ; Larva ; Pest Control ; Polysaccharides
Chemical Substances	Pesticides ; maltodextrin (7CVR7L4A2D) ; Gum Arabic (9000-01-5) ; Biological Control Agents ; Polysaccharides
Language	English
Publishing date	2024-01-29
Publishing country	Germany
Document type	Journal Article
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-023-12990-7
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Article ; Online: Bacillus thuringiensis

He, Xiang / Yang, Yanchao / Soberón, Mario / Bravo, Alejandra / Zhang, Lihong / Zhang, Jie / Wang, Zeyu

Journal of agricultural and food chemistry

2024 Volume 72, Issue 2, Page(s) 1321–1329

Abstract: ... Bacillus ... ...

Abstract	Bacillus thuringiensis
MeSH term(s)	Animals ; Bacillus thuringiensis/chemistry ; Insecticides/chemistry ; Endotoxins/genetics ; Endotoxins/toxicity ; Endotoxins/chemistry ; Protein Domains ; Bacillus thuringiensis Toxins ; Bacterial Proteins/pharmacology ; Bacterial Proteins/toxicity ; Hemolysin Proteins/genetics ; Hemolysin Proteins/toxicity ; Hemolysin Proteins/chemistry ; Larva/metabolism
Chemical Substances	Insecticides ; Endotoxins ; Bacillus thuringiensis Toxins ; Bacterial Proteins ; Hemolysin Proteins
Language	English
Publishing date	2024-01-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	241619-0
ISSN	1520-5118 ; 0021-8561
ISSN (online)	1520-5118
ISSN	0021-8561
DOI	10.1021/acs.jafc.3c08070
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: A major conformational change of N‐terminal helices of Bacillus thuringiensis Cry1Ab insecticidal protein is necessary for membrane insertion and toxicity

Pacheco, Sabino / Gómez Muñoz, Isabel / Soberón, Mario / Bravo, Alejandra

The FEBS Journal. 2023 May, v. 290, no. 10 p.2692-2705

2023

Abstract: Pore forming toxins rely on oligomerization for membrane insertion to kill their targets. Bacillus thuringiensis produces insecticidal Cry‐proteins composed of three domains that form pores that kill the insect larvae. Domain I is involved in ... ...

Abstract	Pore forming toxins rely on oligomerization for membrane insertion to kill their targets. Bacillus thuringiensis produces insecticidal Cry‐proteins composed of three domains that form pores that kill the insect larvae. Domain I is involved in oligomerization and membrane insertion, whereas Domains II and III participate in receptor binding and specificity. However, the structural changes involved in membrane insertion of these proteins remain unsolved. The most widely accepted model for membrane insertion, the ‘umbrella model’, proposed that the α‐4/α‐5 hairpin of Domain I swings away and is inserted into the membrane. To determine the topology of Cry1Ab in the membrane, disulfide bonds linking α‐helices of Domain I were introduced to restrict their movement. Disulfide bonds between helices α‐2/α‐3 or α‐3/α‐4 lost oligomerization and toxicity, indicating that movement of these helices is needed for insecticidal activity. By contrast, disulfide bonds linking helices α‐5/α‐6 did not affect toxicity, which contradicts the ‘umbrella model’. Additionally, Föster resonance energy transfer closest approach analyses measuring distances of different points in the toxin to the membrane plane and collisional quenching assays analysing the protection of specific fluorescent‐labeled residues to the soluble potassium iodide quencher in the membrane inserted state were performed. Overall, the data show that Domain I from Cry1Ab may undergo a major conformational change during its membrane insertion, where the N‐terminal region (helices α‐1 to α‐4) participates in oligomerization and toxicity, probably forming an extended helix. These data break a paradigm, showing a new ‘folding white‐cane model’, which better explains the structural changes of Cry toxins during insertion into the membrane.
Keywords	Bacillus thuringiensis ; disulfides ; energy transfer ; fluorescent labeling ; insecticidal properties ; insecticidal proteins ; insects ; models ; oligomerization ; potassium iodide ; topology ; toxicity ; toxins
Language	English
Dates of publication	2023-05
Size	p. 2692-2705.
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	JOURNAL ARTICLE
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.16710
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Development of an Online Genome Sequence Comparison Resource for

Wang, Kui / Shu, Changlong / Bravo, Alejandra / Soberón, Mario / Zhang, Hongjun / Crickmore, Neil / Zhang, Jie

Toxins

2023 Volume 15, Issue 6

Abstract: An automated method was developed for differentiating closely ... ...

Abstract	An automated method was developed for differentiating closely related
MeSH term(s)	Humans ; Bacillus cereus/genetics ; Multilocus Sequence Typing ; Phylogeny ; Bacillus/genetics ; Bacillus anthracis ; Bacillus thuringiensis/genetics
Language	English
Publishing date	2023-06-12
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2518395-3
ISSN	2072-6651 ; 2072-6651
ISSN (online)	2072-6651
ISSN	2072-6651
DOI	10.3390/toxins15060393
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Article ; Online: Silencing Ditylenchus destructor cathepsin L-like cysteine protease has negative pleiotropic effect on nematode ontogenesis.

Huang, Guoqiang / Cong, Ziwen / Liu, Zhonglin / Chen, Feng / Bravo, Alejandra / Soberón, Mario / Zheng, Jinshui / Peng, Donghai / Sun, Ming

Scientific reports

2024 Volume 14, Issue 1, Page(s) 10030

Abstract: Ditylenchus destructor is a migratory plant-parasitic nematode that severely harms many agriculturally important crops. The control of this pest is difficult, thus efficient strategies for its management in agricultural production are urgently required. ... ...

Abstract	Ditylenchus destructor is a migratory plant-parasitic nematode that severely harms many agriculturally important crops. The control of this pest is difficult, thus efficient strategies for its management in agricultural production are urgently required. Cathepsin L-like cysteine protease (CPL) is one important protease that has been shown to participate in various physiological and pathological processes. Here we decided to characterize the CPL gene (Dd-cpl-1) from D. destructor. Analysis of Dd-cpl-1 gene showed that Dd-cpl-1 gene contains a signal peptide, an I29 inhibitor domain with ERFNIN and GNFD motifs, and a peptidase C1 domain with four conserved active residues, showing evolutionary conservation with other nematode CPLs. RT-qPCR revealed that Dd-cpl-1 gene displayed high expression in third-stage juveniles (J3s) and female adults. In situ hybridization analysis demonstrated that Dd-cpl-1 was expressed in the digestive system and reproductive organs. Silencing Dd-cpl-1 in 1-cell stage eggs of D. destructor by RNAi resulted in a severely delay in development or even in abortive morphogenesis during embryogenesis. The RNAi-mediated silencing of Dd-cpl-1 in J2s and J3s resulted in a developmental arrest phenotype in J3 stage. In addition, silencing Dd-cpl-1 gene expression in female adults led to a 57.43% decrease in egg production. Finally, Dd-cpl-1 RNAi-treated nematodes showed a significant reduction in host colonization and infection. Overall, our results indicate that Dd-CPL-1 plays multiple roles in D. destructor ontogenesis and could serve as a new potential target for controlling D. destructor.
MeSH term(s)	Animals ; Cathepsin L/genetics ; Cathepsin L/metabolism ; RNA Interference ; Female ; Gene Silencing ; Cysteine Proteases/genetics ; Cysteine Proteases/metabolism ; Helminth Proteins/genetics ; Helminth Proteins/metabolism ; Phylogeny ; Tylenchoidea/genetics ; Tylenchoidea/physiology ; Amino Acid Sequence
Chemical Substances	Cathepsin L (EC 3.4.22.15) ; Cysteine Proteases (EC 3.4.-) ; Helminth Proteins
Language	English
Publishing date	2024-05-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-60018-5
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Article ; Online: Identification of Cry toxin receptor genes homologs in a de novo transcriptome of Premnotrypes vorax (Coleoptera: Curculionidae).

Velásquez C, Luisa-Fernanda / Cantón, Pablo Emiliano / Sanchez-Flores, Alejandro / Soberón, Mario / Bravo, Alejandra / Cerón S, Jairo A

PloS one

2023 Volume 18, Issue 9, Page(s) e0291546

Abstract: The white potato worm Premnotrypes vorax (Hustache) (Coleoptera: Curculionidae) is one of the most destructive insect pests of potato crops in South America. Like many coleopteran insects, P. vorax shows low susceptibility to Cry insecticidal proteins ... ...

Abstract	The white potato worm Premnotrypes vorax (Hustache) (Coleoptera: Curculionidae) is one of the most destructive insect pests of potato crops in South America. Like many coleopteran insects, P. vorax shows low susceptibility to Cry insecticidal proteins produced by the bacterium Bacillus thuringiensis (Bt). However, the presence of Cry toxin receptors in the midgut of this this insect has never been studied. The main Cry-binding proteins described in other insect species are cadherin (CAD), aminopeptidase N (APN), alkaline phosphatase (ALP) and ATP-binding cassette (ABC) transporters. In this study, we analyzed and validated a de novo assembled transcriptome of Illumina sequencing data to identify and to characterize homologs of Cry toxin receptors. We identified the protein sequences in P. vorax that show high identity with their orthologous sequences of the Cry toxin binding proteins in other coleopteran larvae such as APN, ALP, CAD and ABC transporter. This study provides preliminary identification of putative receptor genes of Cry proteins that would be useful for future studies involving biocontrol of this important potato crop pest.
MeSH term(s)	Animals ; Coleoptera ; Weevils/genetics ; Transcriptome ; Insect Proteins/genetics ; ATP-Binding Cassette Transporters ; Alkaline Phosphatase ; CD13 Antigens/genetics ; Cadherins ; Coloring Agents
Chemical Substances	Cry toxin receptors ; Insect Proteins ; ATP-Binding Cassette Transporters ; Alkaline Phosphatase (EC 3.1.3.1) ; CD13 Antigens (EC 3.4.11.2) ; Cadherins ; Coloring Agents
Language	English
Publishing date	2023-09-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0291546
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