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 3312
Special Issue Editors
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
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
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
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Keywords
- mode of action
- bacterial toxins
- cry proteins
- Vip proteins
- insecticidal proteins
- functional assays
- binding to receptors
- cross-resistance
- Bacillus thuringiensis
- resistance mechanism
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.