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Related Experiment Video

Updated: May 21, 2025

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

Data-driven evaluation of suitable immunogens for improved antibody selection.

Katharina Waury^1,2, Hlin Kvartsberg^3,4, Henrik Zetterberg^3,4,5,6,7,8

¹Department of Computer Science, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands.

Protein Science : a Publication of the Protein Society

|March 21, 2025

Summary

Selecting the right protein fragments, or immunogens, for antibody production is key. Shorter immunogens with disordered regions and coil stretches yield successful antibodies, while beta sheets and disulfide bridges hinder performance.

Keywords:

Human Protein Atlas antibody antigen disorder immunogen protein structure

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Last Updated: May 21, 2025

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

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Published on: March 25, 2014

Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries

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Published on: January 17, 2015

Antigenic Liposomes for Generation of Disease-specific Antibodies

Antigenic Liposomes for Generation of Disease-specific Antibodies

Published on: October 25, 2018

Area of Science:

Immunology and Biotechnology
Bioinformatics and Computational Biology

Background:

Antibodies are crucial reagents in research and clinical settings due to their specific antigen-binding capabilities.
The selection of optimal protein fragments (immunogens) for antibody generation is a significant challenge, impacting research reproducibility.

Purpose of the Study:

To systematically evaluate immunogen properties influencing antibody production success and specificity.
To identify key structural and functional characteristics of immunogens that correlate with antibody performance.
To develop a tool to aid researchers in selecting suitable immunogens for antibody development.

Main Methods:

Utilized the Human Protein Atlas to analyze immunogen properties.
Classified antibodies as successful or unsuccessful based on standardized validation experiments.
Performed structural and functional analysis of immunogen sequences, including length, secondary structure, and post-translational modification sites.

Main Results:

Shorter immunogens (≤50 residues) with disordered N/C-termini and long coil regions were associated with higher success rates.
Immunogens rich in beta sheets, transmembrane regions, or disulfide bridges correlated with poorer antibody performance.
Post-translational modification sites within immunogens indicated potentially beneficial regions for antibody generation.

Conclusions:

Immunogen characteristics significantly influence antibody success and specificity.
Developed the R package 'immunogenViewer' to assist researchers in selecting optimal immunogens.
Improved immunogen selection can enhance antibody reliability and reproducibility in scientific research.