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Construction of Synthetic Phage Displayed Fab Library with Tailored Diversity

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Recombining germline-derived CDR sequences for creating diverse single-framework antibody libraries.

E Söderlind¹, L Strandberg, P Jirholt

¹BioInvent Therapeutic AB, Lund, Sweden. es@bioinvent.com

Nature Biotechnology

|August 10, 2000

Summary

This summary is machine-generated.

Researchers created a novel antibody library enabling diverse human gene fragments (CDRs) to be combined. Selected antibody fragments showed high affinity, with potential for reduced immunogenicity and increased functional variation.

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

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Published on: January 15, 2020

Area of Science:

Immunology
Molecular Biology
Biotechnology

Background:

Antibody engineering aims to create therapeutic molecules with enhanced specificity and reduced immunogenicity.
Current methods for generating antibody diversity can be limited in scope and efficiency.

Purpose of the Study:

To develop a versatile single-chain variable fragment (scFv) antibody library for combinatorial incorporation of human complementarity-determining region (CDR) gene fragments.
To assess the binding affinity and potential immunogenicity of antibodies generated from this library.

Main Methods:

Construction of a large scFv library (2 x 10^9 transformants) using VH-DP47 and VL-DPL3 frameworks.
Combinatorial assembly of diverse human germline CDR gene fragments into the antibody framework.
Screening of the library against various antigens (haptens, peptides, carbohydrates, proteins).

Main Results:

Selected antibody fragments demonstrated high-affinity binding with dissociation constants in the subnanomolar range.
Antibodies derived from in vivo-processed gene sequences showed potentially lower computed immunogenicity compared to naive immunoglobulins.
The modular assembly process allowed simultaneous variation of up to six CDRs, generating significant genetic and functional diversity.

Conclusions:

The developed antibody library enables efficient generation of high-affinity antibodies with tunable properties.
This approach offers a powerful platform for antibody discovery and engineering, potentially leading to improved therapeutic agents.
The modular design facilitates the creation of antibodies with optimized functionality and reduced immunogenic potential.