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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...

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...

Antibody Structure and Classes

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.

Affinity and Avidity

Affinity and Avidity

Antibody Actions

Antibody Actions

Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...

Diversity of Antigen Receptors

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...

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Related Experiment Video

Updated: Jul 12, 2026

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

Published on: September 14, 2018

Designed ankyrin repeat proteins as anti-idiotypic-binding molecules.

Monique Vogel¹, Elsbeth Keller-Gautschi, Michael J Baumann

¹Institute of Immunology, Inselspital, 3010 Bern, Switzerland. Monique.vogel@iib.unibe.ch

Annals of the New York Academy of Sciences

|September 6, 2007

Summary

Designed ankyrin repeat proteins (DARPins) can act as anti-idiotypic antibodies, regulating immune responses. These novel DARPins inhibit specific antibody binding and function, showing potential as vaccine candidates.

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Area of Science:

Immunology
Protein Engineering

Background:

Antibodies can function as antigens, leading to anti-idiotypic antibodies that regulate immune responses.
Designed ankyrin repeat proteins (DARPins) are emerging as a potential alternative to antibodies in therapeutic applications.

Purpose of the Study:

To investigate the potential of DARPins as anti-idiotypic agents.
To select and characterize DARPins that bind to the idiotype of a specific murine monoclonal antibody (BSW17).

Main Methods:

Selection of DARPins from large libraries against the variable region of anti-human IgE antibody BSW17.
Affinity and binding characteristic analysis of selected DARPins.
In vitro cell assays to evaluate the inhibitory effects of DARPins on BSW17 binding and function.

Main Results:

Two highly specific anti-idiotypic DARPins with high affinity were successfully selected.
The binding characteristics of these DARPins were comparable to a previously identified anti-idiotypic antibody.
The selected DARPins effectively inhibited the binding of BSW17 to cell-bound IgE and its functional activity.

Conclusions:

Anti-idiotypic DARPins can be generated to recognize specific idiotype determinants, analogous to antibodies.
These DARPins demonstrate potential for regulating immune responses and may serve as future vaccine candidates.