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Related Experiment Video

Updated: Aug 26, 2025

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

Published on: October 15, 2016

Fast-tracking antibody maturation using a B cell-based display system.

Hitomi Masuda¹, Atsushi Sawada¹, Shu-Ichi Hashimoto¹

¹Research Laboratories, Chiome Bioscience Inc, Tokyo, Japan.

|October 6, 2022

Summary

This summary is machine-generated.

This study engineered a chicken B cell line for antibody affinity maturation, achieving significant binding improvements in therapeutic antibodies. The versatile system optimizes antibodies from various species efficiently in one round.

Keywords:

Affinity maturation DT40 activation-induced cytidine deaminase coldspot deep sequencing hotspot somatic hypermutation therapeutic antibodies

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Last Updated: Aug 26, 2025

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

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Published on: October 15, 2016

Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood

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Published on: February 6, 2018

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Published on: January 17, 2015

Area of Science:

Biotechnology
Immunology
Molecular Biology

Background:

Affinity maturation is key for therapeutic antibody development.
Current methods like cell display with somatic hypermutation (SHM) require multiple selection rounds.
The human ADLib® system uses autonomous, activation-induced cytidine deaminase (AID)-mediated diversification in DT40 cells.

Purpose of the Study:

To engineer the DT40 cell line for affinity maturation of exogenous antibody genes.
To evaluate the system's efficiency in improving antibody binding affinities.
To demonstrate the system's versatility across different antibody origins.

Main Methods:

Engineered DT40 B cell line to accept exogenous antibody genes.
Introduced immunoglobulin genes from human anti-hVEGF-A antibodies.
Tested affinity maturation with a mouse hybridoma-derived anti-hCDCP1 antibody.

Main Results:

Achieved up to 76.4-fold improvement in binding affinities for human IgG1 antibodies in one round.
Successfully improved affinity of a mouse hybridoma-derived antibody.
Demonstrated retained efficacy and stability in post-humanized antibodies.

Conclusions:

The engineered DT40 B cell-based system is a versatile and efficient tool for antibody optimization.
The system streamlines antibody generation and optimization, regardless of antibody species of origin.
This platform facilitates rapid development of high-affinity therapeutic antibodies.