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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...

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Updated: Jun 22, 2026

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes

Published on: March 25, 2014

Computational structure-based approach to study chimeric antigens using a new protein scaffold displaying foreign

Luigia Cappelli^1,2, Paolo Cinelli^1,2, Andrea Perrotta^2,3

¹Dipartimento di Farmacia e Biotecnologie - FaBiT, University of Bologna, Bologna, Italy.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology

|November 29, 2023

Summary

Researchers engineered a novel protein scaffold using Domain 3 (D3) from Group B Streptococcus (GBS) to display pathogen epitopes for vaccine development. This antigen dissection strategy successfully identified immunogenic loops from Neisseria gonorrhoeae membrane proteins.

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Identification of Functional Protein Regions Through Chimeric Protein Construction

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

Area of Science:

Structural biology
Vaccine development
Protein engineering

Background:

Recombinant production of pathogen outer membrane proteins for vaccines is challenging due to hydrophobic regions.
Only extracellular loops of membrane proteins are typically exposed to the immune system.
Developing effective protein-based vaccines requires functional antigen identification and production.

Purpose of the Study:

To engineer a novel protein scaffold for displaying pathogen extracellular loops.
To identify immunogenic epitopes from Neisseria gonorrhoeae membrane proteins.
To develop a generalized computational approach for epitope design and dissection.

Main Methods:

Computational structure-based design of scaffold and model antigens.
Engineering chimeric proteins using Domain 3 (D3) scaffold and Neisseria gonorrhoeae extracellular loops.
Characterization of chimeric proteins for solubility, stability, and epitope display.
X-ray crystallography to confirm epitope structure.

Main Results:

Successfully produced soluble chimeric D3 proteins displaying extracellular loops of PorB.1b and OpaB.
Identified the most immunogenic extracellular loops from PorB.1b and OpaB.
Obtained crystal structure of a chimeric D3 displaying an immunodominant loop, confirming structural integrity.
Demonstrated D3 as a viable scaffold for epitope insertion and display.

Conclusions:

Domain 3 (D3) serves as a novel and effective protein scaffold for displaying pathogen epitopes.
Antigen dissection and chimeric protein strategies facilitate the identification of immunogenic epitopes.
This approach offers a promising alternative to producing challenging whole membrane proteins for vaccine development.