Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin
Abstract
:1. Introduction
2. Receptor Interactions
2.1. Role of Receptors
2.2. Comparison of ABCC2 and Cadherin as a Cry Protein–Receptor
2.2.1. Generality as a Receptor across Cry Protein Family
2.2.2. Binding Sites on Cry1Aa
2.2.3. Correlation between Binding Affinity to Cry Protein and Mediating Toxicity
2.2.4. Contributions to Cry Susceptibility of Insect Individuals
2.3. APN and ALP
2.3.1. Roles of APN and ALP in General
2.3.2. Role of APNs in Plutella
3. Oligomerization, Membrane Insertion, and Pore Formation
3.1. Mechanisms of Oligomerization
3.2. The “Prepore” and Pore
3.3. Pore Formation via ABCC2 and Cadherin
3.4. Factors Generating the Difference in Pore Formation Efficiency between ABCC2 and Cadherin
3.5. Synergism between ABCC2/C3 and Cadherin in Inducing Efficient Pore Formation
3.5.1. A Molecular Model of the Synergism
3.5.2. Explanation and Prediction of Synergism-Mediated Cry Toxicity Based on Binding Kinetics
4. Model for Pore Formation of Cry Protein via Receptor Interaction
5. Future Perspectives
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Endo, H. Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin. Toxins 2022, 14, 433. https://doi.org/10.3390/toxins14070433
Endo H. Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin. Toxins. 2022; 14(7):433. https://doi.org/10.3390/toxins14070433
Chicago/Turabian StyleEndo, Haruka. 2022. "Molecular and Kinetic Models for Pore Formation of Bacillus thuringiensis Cry Toxin" Toxins 14, no. 7: 433. https://doi.org/10.3390/toxins14070433