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Antibodies 2015, 4(2), 103-122; doi:10.3390/antib4020103

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.
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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)
View Full-Text   |   Download PDF [2169 KB, uploaded 20 May 2015]   |  

Abstract

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
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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).

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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.

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