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Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

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Updated: Jun 17, 2026

Detection of True IgE-expressing Mouse B Lineage Cells

Detection of True IgE-expressing Mouse B Lineage Cells

Published on: December 1, 2014

Structural correlates of mouse IgA allotypes.

Julia M Phillips-Quagliata¹

¹Department of Pathology, New York University School of Medicine, New York, NY 10016, USA. phillj01@med.nyu.edu

|December 17, 2009

Summary

This summary is machine-generated.

Mouse immunoglobulin A (IgA) allotypes were engineered to study alpha-chain and light-chain binding. Unique amino acid differences in IgA allotypes determine covalent bonding and antibody binding site interactions.

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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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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

Area of Science:

Immunology
Molecular Biology
Protein Chemistry

Background:

Immunoglobulin A (IgA) is a crucial antibody isotype involved in mucosal immunity.
Allotypic variations in IgA alpha-chains can influence its structure and function.
Understanding these variations is key to deciphering IgA-mediated immune responses.

Purpose of the Study:

To investigate the structural and functional consequences of amino acid differences among mouse IgA alpha-chain allotypes.
To identify specific amino acids responsible for covalent alpha- and light-chain (L-chain) bonding.
To map allotypic epitopes recognized by monoclonal antibodies.

Main Methods:

Site-directed mutagenesis of an S107-IgA plasmid to create variant alpha-chains.
Transfection of myeloma cells with engineered IgA and kappa-chain plasmids.
Analysis of secreted IgA for covalent alpha-L-chain linkage and binding to anti-allotypic antibodies (HIS-M2, HY-15, HY-16).

Main Results:

IgA of the Igh-2(a) allotype uniquely lacks a covalent alpha-L-chain bond, dependent on an "extra" Cys in other allotypes.
Specific amino acids in the Calpha1 region dictate binding to anti-allotypic antibodies.
HIS-M2 binding requires Ala 216; HY-15 binding requires Pro 216 and Asp 222; HY-16 binding requires Arg 183 and Pro/Ser 216 (not Ala 216).
Defective glycosylation in transfectants impaired HY-16 binding, necessitating deglycosylation for detection.

Conclusions:

Amino acid sequence variations in mouse IgA alpha-chains significantly impact inter-chain covalent bonding.
Specific residues within the Calpha1 domain are critical for defining allotypic epitopes and antibody recognition.
Glycosylation status can influence the detection of allotypic interactions.