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Cross-reactivity

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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...

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...

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...

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.

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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

B-cell epitopes: Discontinuity and conformational analysis.

Saba Ferdous¹, Sebastian Kelm², Terry S Baker²

¹Institute of Structural and Molecular Biology, Division of Biosciences, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.

Molecular Immunology

|September 24, 2019

Summary

This summary is machine-generated.

Most B-cell epitopes are discontinuous, posing challenges for vaccine design. This study analyzes epitope structures, identifying regions and fragments to understand their conformational nature for improved peptide vaccine development.

Keywords:

Antibody–antigen interactions Antigen Discontinuous epitopes Epitope conformation Protein conformation Protein structure

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Area of Science:

Immunology
Vaccinology
Structural Biology

Background:

Peptide vaccines offer advantages like cost-effectiveness and stability.
The discontinuous nature of most B-cell epitopes (BCEs) hinders vaccine development.
Mimicking native BCEs is crucial for effective vaccine design.

Purpose of the Study:

To analyze the discontinuity and conformational properties of B-cell epitopes.
To develop computational methods for classifying epitope structures.
To inform the design of peptide vaccines that better mimic natural epitopes.

Main Methods:

Defined 'regions' and 'fragments' based on antibody-contacting residues.
Developed an algorithm to classify epitope region shapes (straight, curved, folded).
Analyzed the structural characteristics of 488 B-cell epitopes.

Main Results:

Identified 1282 regions and 1018 fragments across 488 B-cell epitopes.
Found that 90% of epitopes contain five or fewer regions and fragments.
Classified 508 regions as straight, 626 as curved, and 148 as folded.

Conclusions:

Epitope discontinuity and conformational shape are key factors in peptide vaccine design.
Understanding these structural features can guide the creation of more immunogenic peptide vaccines.
The developed classification algorithm aids in characterizing epitopes for vaccine development.