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Biomolecules
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Identification and Characterization of Receptors for Bacillus thuringiensis Pesticidal Toxins
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Identification and Characterization of Receptors for Bacillus thuringiensis Pesticidal Toxins

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 31 October 2024 | Viewed by 3236

Special Issue Editors

Dr. Patricia Hernández-Martínez

E-Mail Website
Guest Editor
Instituto de Biotecnología y Biomedicina (BIOTECMED), Department of Genetics, Universitat de València, 46100 Burjassot, Spain
Interests: understanding the mechanisms by which Bacillus thuringiensis toxins exert their toxicity (mode of action), and how insects can develop resistance to them; understanding the response mechanisms of insects to B. thuringiensis proteins exposure
Special Issues, Collections and Topics in MDPI journals
Dr. Yolanda Bel

E-Mail Website
Guest Editor
Instituto de Biotecnología y Biomedicina (BIOTECMED), Department of Genetics, Universitat de València, 46100 Burjassot, Spain
Interests: research on new Bt strains and their insecticidal and nematocidal protein genes for the development of new Bt-based strategies to control agricultural pests; biochemical and genetic bases of resistance to Bacillus thuringiensis (Bt) and mode of action of its proteins; molecular markers of Bt resistance genes
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Juan Ferré

E-Mail Website
Guest Editor
Instituto de Biotecnología y Biomedicina (BIOTECMED), Department of Genetics, Universitat de València, 46100 Burjassot, Spain
Interests: understanding the biochemical and genetic bases of insect resistance to Bacillus thuringiensis toxins; to study the mode of action of Vip3 insecticidal proteins
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Bacillus thuringiensis (Bt) produces a variety of proteins with specific toxicities that have been proven to be effective against a wide range of insect orders, nematodes, and human cancer cells. Furthermore, these proteins have the added advantage of being safe for mammals and other non-target insects, making them highly suitable for use as insecticides in the form of sprays or in genetically modified Bt crops. Currently, some 3d-Cry and Vip3 proteins are extensively used to control insect pests and vectors. However, the ongoing use of this natural and safe insect control method is threatened due to the development of insect resistance, especially to 3d-Cry proteins. Currently, binding site alteration is the most common mechanism associated with high levels of insect resistance.

The aim of this Special Issue is to gather information that will expand the of knowledge of the molecules that act as functional receptors of the different pesticidal Bt proteins. Additionally, we welcome studies that characterize whether different Bt proteins which are toxic for a target pest share the same binding sites, even if the molecular identities of these binding sites are still unknown, as they are valuable to predict risks of cross-resistance among these proteins. We are also interested in studies on the alterations in receptor proteins that limit their functionality, leading to resistance to the corresponding Bt proteins. Understanding the mechanisms developed by susceptible hosts to counteract the toxic effects of Bt proteins can help scientists to design better strategies to maintain the long-term efficiency of Bt-based products.

Dr. Patricia Hernández-Martínez
Dr. Yolanda Bel
Prof. Dr. Juan Ferré
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • mode of action
  • bacterial toxins
  • cry proteins
  • Vip proteins
  • insecticidal proteins
  • functional assays
  • binding to receptors
  • cross-resistance
  • Bacillus thuringiensis
  • resistance mechanism

Published Papers (4 papers)

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Research

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10 pages, 3817 KiB  
Article
New Paralogs of the Heliothis virescens ABCC2 Transporter as Potential Receptors for Bt Cry1A Proteins
by Daniel Pinos, Anabel Millán-Leiva, Juan Ferré and Patricia Hernández-Martínez
Biomolecules 2024, 14(4), 397; https://doi.org/10.3390/biom14040397 - 26 Mar 2024
Viewed by 588
Abstract
The ATP-binding cassette (ABC) transporters are a superfamily of membrane proteins. These active transporters are involved in the export of different substances such as xenobiotics. ABC transporters from subfamily C (ABCC) have also been described as functional receptors for different insecticidal proteins from [...] Read more.
The ATP-binding cassette (ABC) transporters are a superfamily of membrane proteins. These active transporters are involved in the export of different substances such as xenobiotics. ABC transporters from subfamily C (ABCC) have also been described as functional receptors for different insecticidal proteins from Bacillus thuringiensis (Bt) in several lepidopteran species. Numerous studies have characterized the relationship between the ABCC2 transporter and Bt Cry1 proteins. Although other ABCC transporters sharing structural and functional similarities have been described, little is known of their role in the mode of action of Bt proteins. For Heliothis virescens, only the ABCC2 transporter and its interaction with Cry1A proteins have been studied to date. Here, we have searched for paralogs to the ABCC2 gene in H. virescens, and identified two new ABC transporter genes: HvABCC3 and HvABCC4. Furthermore, we have characterized their gene expression in the midgut and their protein topology, and compared them with that of ABCC2. Finally, we discuss their possible interaction with Bt proteins by performing protein docking analysis. Full article
(This article belongs to the Special Issue Identification and Characterization of Receptors for Bacillus thuringiensis Pesticidal Toxins)
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20 pages, 10146 KiB  
Article
Cry Toxins Use Multiple ATP-Binding Cassette Transporter Subfamily C Members as Low-Efficiency Receptors in Bombyx mori
by Satomi Adegawa, Yonghao Wang, Ryusei Waizumi, Tetsuya Iizuka, Yoko Takasu, Kenji Watanabe and Ryoichi Sato
Biomolecules 2024, 14(3), 271; https://doi.org/10.3390/biom14030271 - 23 Feb 2024
Cited by 1 | Viewed by 756
Abstract
Recent studies have suggested that ABC transporters are the main receptors of Cry toxins. However, the receptors of many Cry toxins have not been identified. In this study, we used a heterologous cell expression system to identify Bombyx mori ABC transporter subfamily C [...] Read more.
Recent studies have suggested that ABC transporters are the main receptors of Cry toxins. However, the receptors of many Cry toxins have not been identified. In this study, we used a heterologous cell expression system to identify Bombyx mori ABC transporter subfamily C members (BmABCCs) that function as receptors for five Cry toxins active in Lepidopteran insects: Cry1Aa, Cry1Ca, Cry1Da, Cry8Ca, and Cry9Aa. All five Cry toxins can use multiple ABCCs as low-efficiency receptors, which induce cytotoxicity only at high concentrations. Surface plasmon resonance analysis revealed that the KD values between the toxins and BmABCC1 and BmABCC4 were 10−5 to 10−9 M, suggesting binding affinities 8- to 10,000-fold lower than those between Cry1Aa and BmABCC2, which are susceptibility-determining receptors for Cry1Aa. Bioassays in BmABCC-knockout silkworm strains showed that these low-efficiency receptors are not involved in sensitivity to Cry toxins. The findings suggest that each family of Cry toxins uses multiple BmABCCs as low-efficiency receptors in the insect midgut based on the promiscuous binding of their receptor-binding regions. Each Cry toxin seems to have evolved to utilize one or several ABC transporters as susceptibility-determining receptors. Full article
(This article belongs to the Special Issue Identification and Characterization of Receptors for Bacillus thuringiensis Pesticidal Toxins)
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21 pages, 3976 KiB  
Article
Culex quinquefasciatus Resistant to the Binary Toxin from Lysinibacillus sphaericus Displays a Consistent Downregulation of Pantetheinase Transcripts
by Tatiana M. T. Rezende, Heverly S. G. Menezes, Antonio M. Rezende, Milena P. Cavalcanti, Yuri M. G. Silva, Osvaldo P. de-Melo-Neto, Tatiany P. Romão and Maria Helena N. L. Silva-Filha
Biomolecules 2024, 14(1), 33; https://doi.org/10.3390/biom14010033 - 25 Dec 2023
Viewed by 890
Abstract
Culex quinquefasciatus resistance to the binary (Bin) toxin, the major larvicidal component from Lysinibacillus sphaericus, is associated with mutations in the cqm1 gene, encoding the Bin-toxin receptor. Downregulation of the cqm1 transcript was found in the transcriptome of larvae resistant to the [...] Read more.
Culex quinquefasciatus resistance to the binary (Bin) toxin, the major larvicidal component from Lysinibacillus sphaericus, is associated with mutations in the cqm1 gene, encoding the Bin-toxin receptor. Downregulation of the cqm1 transcript was found in the transcriptome of larvae resistant to the L. sphaericus IAB59 strain, which produces both the Bin toxin and a second binary toxin, Cry48Aa/Cry49Aa. Here, we investigated the transcription profiles of two other mosquito colonies having Bin resistance only. These confirmed the cqm1 downregulation and identified transcripts encoding the enzyme pantetheinase as the most downregulated mRNAs in both resistant colonies. Further quantification of these transcripts reinforced their strong downregulation in Bin-resistant larvae. Multiple genes were found encoding this enzyme in Cx. quinquefasciatus and a recombinant pantetheinase was then expressed in Escherichia coli and Sf9 cells, with its presence assessed in the midgut brush border membrane of susceptible larvae. The pantetheinase was expressed as a ~70 kDa protein, potentially membrane-bound, which does not seem to be significantly targeted by glycosylation. This is the first pantetheinase characterization in mosquitoes, and its remarkable downregulation might reflect features impacted by co-selection with the Bin-resistant phenotype or potential roles in the Bin-toxin mode of action that deserve to be investigated. Full article
(This article belongs to the Special Issue Identification and Characterization of Receptors for Bacillus thuringiensis Pesticidal Toxins)
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Review

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18 pages, 10449 KiB  
Review
Utilization of Diverse Molecules as Receptors by Cry Toxin and the Promiscuous Nature of Receptor-Binding Sites Which Accounts for the Diversity
by Ryoichi Sato
Biomolecules 2024, 14(4), 425; https://doi.org/10.3390/biom14040425 - 01 Apr 2024
Viewed by 636
Abstract
By 2013, it had been shown that the genes cadherin-like receptor (Cad) and ATP-binding cassette transporter subfamily C2 (ABCC2) were responsible for insect resistance to several Cry1A toxins, acting as susceptibility-determining receptors, and many review articles have been published. Therefore, this review focuses [...] Read more.
By 2013, it had been shown that the genes cadherin-like receptor (Cad) and ATP-binding cassette transporter subfamily C2 (ABCC2) were responsible for insect resistance to several Cry1A toxins, acting as susceptibility-determining receptors, and many review articles have been published. Therefore, this review focuses on information about receptors and receptor-binding sites that have been revealed since 2014. Since 2014, studies have revealed that the receptors involved in determining susceptibility vary depending on the Cry toxin subfamily, and that binding affinity between Cry toxins and receptors plays a crucial role. Consequently, models have demonstrated that ABCC2, ABCC3, and Cad interact with Cry1Aa; ABCC2 and Cad with Cry1Ab and Cry1Ac; ABCC2 and ABCC3 with Cry1Fa; ABCB1 with Cry1Ba, Cry1Ia, Cry9Da, and Cry3Aa; and ABCA2 with Cry2Aa and Cry2Ba, primarily in the silkworm, Bombyx mori. Furthermore, since 2017, it has been suggested that the binding sites of BmCad and BmABCC2 on Cry1Aa toxin overlap in the loop region of domain II, indicating that Cry toxins use various molecules as receptors due to their ability to bind promiscuously in this region. Additionally, since 2017, several ABC transporters have been identified as low-efficiency receptors that poorly induce cell swelling in heterologously expressing cultured cells. In 2024, research suggested that multiple molecules from the ABC transporter subfamily, including ABCC1, ABCC2, ABCC3, ABCC4, ABCC10, and ABCC11, act as low-efficiency receptors for a single Cry toxin in the midgut of silkworm larvae. This observation led to the hypothesis that the presence of such low-efficiency receptors contributes to the evolution of Cry toxins towards the generation of highly functional receptors that determine the susceptibility of individual insects. Moreover, this evolutionary process is considered to offer valuable insights for the engineering of Cry toxins to overcome resistance and develop countermeasures against resistance. Full article
(This article belongs to the Special Issue Identification and Characterization of Receptors for Bacillus thuringiensis Pesticidal Toxins)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: undetermined
Authors: Yolanda Bel
Affiliation: ERI de Biotecnología y Biomedicina (BIOTECMED), Department of Genetics, Universitat de València, 46100 Burjassot, Spain
Abstract: Bt-cadherins, a particular type of midgut cadherins, act as receptors for Bacillus thuringiensis Cry1A pesticidal proteins. The aim of this work was to identify and validate the candidate Cry1A cadherin receptor in Grapholita molesta (GmCad1). The GmCad1 gene was identified through genome mining using lepidopteran Bt-related cadherins and phylogenetic analyses grouped GmCad1 with other Torticidae cadherins, in a different clade than the lepidopteran Bt-related cadherins. In silico analysis of the GmCad1 showed a structure similar to Bt-related cadherins, with 11 cadherin repeats (CRs), a transmembrane region, and an intracellular domain. The in vivo occurrence of the GmCad1 transcript was confirmed in G. molesta guts through PCR amplification. To validate the binding ability of Cry1A proteins to GmCad1, a sequence comprising the cadherin fragment CR7-CR11 was expressed and assayed in vitro for toxin binding. The results showed that Cry1A proteins bind to this region in a dose-dependent manner. In silico molecular docking analysis suggests that the interaction may involve mainly the Domains II of Cry1Ab and Cry1Ac, and the Domain III of Cry1Aa. This study provides the first evidence of a 99-C cadherin serving as a receptor for Cry1A in G. molesta.

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