Next Article in Journal
Reverse Signaling Contributes to Control of Chronic Inflammation by Anti-TNF Therapeutics
Previous Article in Journal
Codon-Precise, Synthetic, Antibody Fragment Libraries Built Using Automated Hexamer Codon Additions and Validated through Next Generation Sequencing
Previous Article in Special Issue
A Monoclonal Antibody to Human DLK1 Reveals Differential Expression in Cancer and Absence in Healthy Tissues
Article Menu

Export Article

Open AccessArticle
Antibodies 2015, 4(2), 103-122;

Purpose-Oriented Antibody Libraries Incorporating Tailored CDR3 Sequences

Novimmune S.A., 14 chemin des Aulx 1228 Plan-les-Ouates, Switzerland
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Ahuva Nissim
Received: 10 March 2015 / Revised: 17 April 2015 / Accepted: 12 May 2015 / Published: 20 May 2015
(This article belongs to the Special Issue Antibody Gene Libraries)
Full-Text   |   PDF [2169 KB, uploaded 20 May 2015]   |  


The development of in vitro antibody selection technologies has allowed overcoming some limitations inherent to the hybridoma technology. In most cases, large repertoires of antibody genes have been assembled to create highly diversified libraries allowing the isolation of antibodies recognizing virtually any antigen. However, these universal libraries might not allow the isolation of antibodies with specific structural properties or particular amino acid contents that are rarely found in natural repertoires. Purpose-oriented libraries specially designed to incorporate desired characteristics have been successfully used. However, the workload required for library construction has limited the attractiveness of this approach compared to the use of large universal libraries. We have developed an approach to capture synthetic or natural diversity into the complementarity determining regions 3 (CDR3) of human antibody repertoires using Type IIS restriction enzymes. In this way, we generated several libraries either biased in amino acid content or towards long CDRH3 loops. The latter were successfully used to identify antibodies inhibiting the enzymatic activity of horseradish peroxidase, whereas libraries enriched in histidines allowed for the isolation of antibodies binding to human Fc in a pH-dependent manner. These libraries indicate that tailored diversification of CDR3 is sufficient to generate purpose-oriented libraries and isolate antibodies with uncommon properties. View Full-Text
Keywords: monoclonal antibody; phage display; antibody library; complementary determining region; cryptic site; pH-dependence monoclonal antibody; phage display; antibody library; complementary determining region; cryptic site; pH-dependence

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Bonvin, P.; Venet, S.; Kosco-Vilbois, M.; Fischer, N. Purpose-Oriented Antibody Libraries Incorporating Tailored CDR3 Sequences. Antibodies 2015, 4, 103-122.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Antibodies EISSN 2073-4468 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top