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Updated: Jun 6, 2025
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Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
Published on: April 17, 2017
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A non-classical view of antibody properties: Allosteric effect between variable and constant regions
Xiaoting Yu1, Huiling Zhang2, Tao Zhou1
1Guangdong Provincial Key Laboratory of Food Quality and Safety, College of Food Science, South China Agricultural University, Guangzhou 510642, China.
Biotechnology Advances
|November 23, 2024
Summary
Antibodies are not just two separate parts; their variable and constant regions communicate via allostery. Understanding this antibody allostery is key for advanced antibody engineering and vaccine design.
Area of Science:
- Immunology
- Structural Biology
- Biotechnology
Background:
- Antibodies traditionally viewed as having independent variable (V) and constant (C) regions.
- Classical model posits V regions for antigen binding and C regions for effector functions.
Purpose of the Study:
- To review and synthesize current research on antibody allostery.
- To explore the transmission of allosteric signals between V and C regions.
- To advocate for a revised understanding of antibody structure-function relationships.
Main Methods:
- Comprehensive literature review of studies on antibody allostery.
- Analysis of conformational changes induced by covalent modifications and ligand binding.
- Examination of intramolecular signal transmission pathways.
Main Results:
- Growing evidence challenges the functional independence of V and C regions.
- Allosteric interactions link V and C regions through long-range conformational changes.
- Both covalent modifications and ligand binding can induce allosteric effects.
Conclusions:
- Antibody allostery provides a new framework for understanding antibody structure-function.
- Insights from antibody allostery offer predictable methods for regulating antibody functions.
- Advances in antibody allostery will significantly impact antibody engineering and vaccine design.
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