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Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin
Cry proteins from Bacillus thuringiensis (Bt) and other bacteria are pesticidal pore-forming toxins. Since 2010, when the ABC transporter C2 (ABCC2) was identified as a Cry1Ac protein resistant gene, our understanding of the mode of action of Cry protein has progressed substantially. ABCC2 mediates...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9321905/ https://www.ncbi.nlm.nih.gov/pubmed/35878171 http://dx.doi.org/10.3390/toxins14070433 |
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author | Endo, Haruka |
author_facet | Endo, Haruka |
author_sort | Endo, Haruka |
collection | PubMed |
description | Cry proteins from Bacillus thuringiensis (Bt) and other bacteria are pesticidal pore-forming toxins. Since 2010, when the ABC transporter C2 (ABCC2) was identified as a Cry1Ac protein resistant gene, our understanding of the mode of action of Cry protein has progressed substantially. ABCC2 mediates high Cry1A toxicity because of its high activity for helping pore formation. With the discovery of ABCC2, the classical killing model based on pore formation and osmotic lysis became nearly conclusive. Nevertheless, we are still far from a complete understanding of how Cry proteins form pores in the cell membrane through interactions with their host gut membrane proteins, known as receptors. Why does ABCC2 mediate pore formation with high efficiency unlike other Cry1A-binding proteins? Is the “prepore” formation indispensable for pore formation? What is the mechanism underlying the synergism between ABCC2 and the 12-cadherin domain protein? We examine potential mechanisms of pore formation via receptor interactions in this paper by merging findings from prior studies on the Cry mode of action before and after the discovery of ABC transporters as Cry protein receptors. We also attempt to explain Cry toxicity using Cry–receptor binding affinities, which successfully predicts actual Cry toxicity toward cultured cells coexpressing ABC transporters and cadherin. |
format | Online Article Text |
id | pubmed-9321905 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-93219052022-07-27 Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin Endo, Haruka Toxins (Basel) Perspective Cry proteins from Bacillus thuringiensis (Bt) and other bacteria are pesticidal pore-forming toxins. Since 2010, when the ABC transporter C2 (ABCC2) was identified as a Cry1Ac protein resistant gene, our understanding of the mode of action of Cry protein has progressed substantially. ABCC2 mediates high Cry1A toxicity because of its high activity for helping pore formation. With the discovery of ABCC2, the classical killing model based on pore formation and osmotic lysis became nearly conclusive. Nevertheless, we are still far from a complete understanding of how Cry proteins form pores in the cell membrane through interactions with their host gut membrane proteins, known as receptors. Why does ABCC2 mediate pore formation with high efficiency unlike other Cry1A-binding proteins? Is the “prepore” formation indispensable for pore formation? What is the mechanism underlying the synergism between ABCC2 and the 12-cadherin domain protein? We examine potential mechanisms of pore formation via receptor interactions in this paper by merging findings from prior studies on the Cry mode of action before and after the discovery of ABC transporters as Cry protein receptors. We also attempt to explain Cry toxicity using Cry–receptor binding affinities, which successfully predicts actual Cry toxicity toward cultured cells coexpressing ABC transporters and cadherin. MDPI 2022-06-24 /pmc/articles/PMC9321905/ /pubmed/35878171 http://dx.doi.org/10.3390/toxins14070433 Text en © 2022 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Perspective Endo, Haruka Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin |
title | Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin |
title_full | Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin |
title_fullStr | Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin |
title_full_unstemmed | Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin |
title_short | Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin |
title_sort | molecular and kinetic models for pore formation of bacillus thuringiensis cry toxin |
topic | Perspective |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9321905/ https://www.ncbi.nlm.nih.gov/pubmed/35878171 http://dx.doi.org/10.3390/toxins14070433 |
work_keys_str_mv | AT endoharuka molecularandkineticmodelsforporeformationofbacillusthuringiensiscrytoxin |