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Related Concept Videos

Antibody Structure01:10

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...
Antibody Structure01:10

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...
Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Transcytosis of IgG01:15

Transcytosis of IgG

Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
Protein Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

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Related Experiment Video

Updated: May 29, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Structure and function relationships in IgA.

J M Woof1, M W Russell

  • 1Medical Research Institute, University of Dundee Medical School, Dundee, UK. j.m.woof@dundee.ac.uk

Mucosal Immunology
|September 23, 2011
PubMed
Summary
This summary is machine-generated.

Human Immunoglobulin A (IgA) is key for mucosal immunity, with unique structures enabling its function. Understanding IgA structure and pathogen interactions is vital for developing new IgA-based therapies.

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Recognition of Epidermal Transglutaminase by IgA and Tissue Transglutaminase 2 Antibodies in a Rare Case of Rhesus Dermatitis
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Recognition of Epidermal Transglutaminase by IgA and Tissue Transglutaminase 2 Antibodies in a Rare Case of Rhesus Dermatitis

Published on: December 15, 2011

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions
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Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions

Published on: July 10, 2021

Related Experiment Videos

Last Updated: May 29, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Recognition of Epidermal Transglutaminase by IgA and Tissue Transglutaminase 2 Antibodies in a Rare Case of Rhesus Dermatitis
10:27

Recognition of Epidermal Transglutaminase by IgA and Tissue Transglutaminase 2 Antibodies in a Rare Case of Rhesus Dermatitis

Published on: December 15, 2011

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions
07:35

Double Labeling Immunofluorescence using Antibodies from the Same Species to Study Host-Pathogen Interactions

Published on: July 10, 2021

Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Medicine

Background:

  • Immunoglobulin A (IgA) is crucial for mucosal immune defense.
  • Its protective function relies on unique structural features and polymerization capabilities.
  • IgA's heavy chain attributes are central to its role in immunity.

Purpose of the Study:

  • To provide an overview of human IgA structure.
  • To describe distinguishing features of IgA1 and IgA2 subclasses.
  • To map host receptor interaction sites and their subversion by pathogens.

Main Methods:

  • Structural analysis of human IgA subclasses.
  • Mapping of IgA interaction sites with host receptors.
  • Review of pathogen-derived proteins and proteases targeting IgA.

Main Results:

  • Detailed description of human IgA1 and IgA2 structural differences.
  • Identification of key interaction sites on IgA for host receptors.
  • Demonstration that pathogens exploit these interaction sites to evade IgA immunity.

Conclusions:

  • Understanding IgA structure-function relationships is critical for mucosal immunity.
  • Pathogen strategies involve targeting IgA interaction sites.
  • Knowledge of IgA structure is invaluable for developing therapeutic IgA-based monoclonal antibodies.