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Related Experiment Video

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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

Published on: March 15, 2019

Variable region identical immunoglobulins differing in isotype express different paratopes.

Alena Janda¹, Ertan Eryilmaz², Antonio Nakouzi¹

¹Department of Microbiology and Immunology, The Albert Einstein College of Medicine, Bronx, New York 10461.

The Journal of Biological Chemistry

|August 30, 2012

Summary

This summary is machine-generated.

Antibody constant regions influence antibody specificity. This study shows how constant regions alter antibody structure, impacting immune responses and vaccine efficacy.

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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing

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Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay

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T and B Cell Receptor Immune Repertoire Analysis using Next-generation Sequencing

T and B Cell Receptor Immune Repertoire Analysis using Next-generation Sequencing

Published on: January 12, 2021

Area of Science:

Immunology
Structural Biology
Biochemistry

Background:

Antibody (Ab) constant (C) region's influence on fine specificity is known but mechanistically unclear.
This phenomenon is crucial for vaccine responses and antibody diversity generation.

Purpose of the Study:

To investigate the molecular mechanism by which antibody C regions affect paratope structure and antigen binding.
To test the hypothesis that C regions impose conformational constraints on variable (V) regions.

Main Methods:

Utilized (15)N-labeled peptide mimetics to probe the antibody paratope.
Employed Nuclear Magnetic Resonance (NMR) spectroscopy and fluorescence emission spectroscopy.
Compared variable region-identical IgG isotypes (IgG1, IgG2a, IgG2b, IgG3) to identify isotype-specific effects.

Main Results:

Observed isotype-related differences in fluorescence emission spectroscopy.
Detected temperature-dependent variations in peptide mimetic binding and cleavage.
Demonstrated that C regions can modify V region conformation.

Conclusions:

The antibody C region actively modulates V region structure, altering the paratope.
This provides a molecular explanation for how antibody isotype influences antigen specificity.
Highlights the role of isotype switching in generating functional antibody diversity.