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Affinity and Avidity

Affinity and Avidity

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

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.

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...

B Cell Activation and Differentiation

B Cell Activation and Differentiation

The adaptive immune response, a sophisticated defense mechanism, relies on the activation and differentiation of B lymphocytes, or B cells. These processes enable our bodies to mount a tailored response against specific pathogens such as bacteria, free virus particles, toxins, and parasites.
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...

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Related Experiment Video

Updated: Apr 16, 2026

Assessing Somatic Hypermutation in Ramos B Cells after Overexpression or Knockdown of Specific Genes

Assessing Somatic Hypermutation in Ramos B Cells after Overexpression or Knockdown of Specific Genes

Published on: November 1, 2011

Adaptive mutations alter antibody structure and dynamics during affinity maturation.

Ramkrishna Adhikary, Wayne Yu, Masayuki Oda¹

¹§Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, 1-5, Hangi-cho, Shimogamo, Sakyo-ku, Kyoto 606-8522, Japan.

|March 11, 2015

Summary

This summary is machine-generated.

Adaptive mutations optimize protein dynamics during antibody affinity maturation. This study reveals how changes in protein mechanics, not just structure, contribute to antibody evolution and function.

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Area of Science:

Protein dynamics and evolution
Molecular recognition and biophysics
Adaptive evolution of proteins

Background:

Adaptive mutations can alter protein function through structural changes.
Protein dynamics play a likely but less understood role in adaptive evolution.
Antibody (Ab) affinity maturation provides a model to study adaptive mutations and protein dynamics.

Purpose of the Study:

To characterize the sequence, molecular recognition, structure, and dynamics of three affinity-matured antibodies (Abs).
To investigate the role of protein dynamics in antibody affinity maturation.
To explore how adaptive mutations influence protein mechanical responses.

Main Methods:

Raised three affinity-matured antibodies from a common germline precursor against 8-methoxypyrene-1,3,6-trisulfonate (MPTS).
Determined the mechanical response of Ab-antigen complexes to applied force using three-pulse photon echo peak shift (3PEPS) spectroscopy.
Deconvoluted mechanical responses into elastic, anelastic, and plastic components.

Main Results:

One Ab achieved affinity maturation via a single functional group contact, showing minimal anelasticity or plasticity.
Two other Abs with multiple mutations, lacking direct contact, exhibited significant changes in anelasticity and plasticity.
Higher plasticity levels correlated with increased specificity, suggesting a role for dynamics in affinity maturation.

Conclusions:

Optimization of protein dynamics, alongside structure, likely contributes to antibody affinity maturation.
Adaptive evolution may involve optimizing both protein structure and dynamics for enhanced function.
Findings suggest a broader role for dynamics in the evolution of other proteins.