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Related Concept Videos

Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
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...
Hybridoma Technology01:31

Hybridoma Technology

Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
Hybridoma Selection
Commonly used fusion techniques — electroporation, polyethylene glycol...
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.

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Related Experiment Video

Updated: May 10, 2026

Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

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

Published on: March 15, 2019

Reshaping antibody diversity.

Feng Wang1, Damian C Ekiert, Insha Ahmad

  • 1Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA.

Cell
|June 11, 2013
PubMed
Summary
This summary is machine-generated.

Cows possess unique antibodies with ultralong CDR H3 loops that form disulfide-bonded minidomains. This structural diversity, generated by somatic hypermutation, enhances the bovine antibody repertoire and antigen recognition.

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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
08:51

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

Published on: March 15, 2019

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Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations
09:07

Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations

Published on: August 22, 2019

Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Biology

Background:

  • Some species exhibit strong antibody responses despite limited genetic diversity.
  • Cattle (Bos taurus) have a unique antibody system characterized by long CDR H3 loops and few V regions, with an unknown diversity generation mechanism.

Purpose of the Study:

  • To investigate the mechanism behind the generation of antibody diversity in cattle, focusing on the unique features of their CDR H3 loops.
  • To elucidate the structural basis and functional implications of ultralong CDR H3s in bovine antibodies.

Main Methods:

  • Deep sequencing of bovine antibody repertoires.
  • Crystal structure determination of bovine antibodies.
  • Analysis of somatic hypermutation patterns and codon bias.

Main Results:

  • Ultralong CDR H3 loops in cattle antibodies contain numerous cysteines, suggesting the formation of disulfide-bonded minidomains.
  • Crystal structures revealed an architecture with a beta strand "stalk" supporting a diverse, disulfide-bonded "knob" domain.
  • Somatic hypermutation of ultralong DH segments, with a bias towards cysteine, drives diversity generation.

Conclusions:

  • The bovine immune system generates antibody diversity through ultralong CDR H3s that fold into minidomains via somatically generated disulfides.
  • These unique antibody structures, particularly the knob domain, can be elicited to recognize specific antigens.
  • Bovine antibodies possess a distinct structural and diversity-generating mechanism compared to other species.