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Selection and identification of single domain antibody fragments from camel heavy‐chain antibodies

FEBS Letters · 1997 · Vol. 414(3) · pp. 521–526
Mehdi Arbabi GhahroudiAline DesmyterL. WynsR. HamersSerge Muyldermans

Abstract

Functional heavy-chain gamma-immunoglobulins lacking light chains occur naturally in Camelidae. We now show the feasibility of immunising a dromedary, cloning the repertoire of the variable domains of its heavy-chain antibodies and panning, leading to the successful identification of minimum sized antigen binders. The recombinant binders are expressed well in E. coli, extremely stable, highly soluble, and react specifically and with high affinity to the antigens. This approach can be viewed as a general route to obtain small binders with favourable characteristics and valuable perspectives as modular building blocks to manufacture multispecific or multifunctional chimaeric proteins.

Monoclonal and Polyclonal Antibodies ResearchProtein purification and stabilityGlycosylation and Glycoproteins ResearchPanning (audio)Recombinant DNAImmunoglobulin light chainAntigenComputational biologyAntibodyBiologyCloning (programming)Heavy chainModular design

MeSH terms

Amino Acid SequenceAnimalsAntibodiesAntibody AffinityAntibody SpecificityBacteriophagesBinding Sites, AntibodyCamelusCloning, MolecularImmunoglobulin Heavy ChainsMolecular Sequence DataRecombinant ProteinsGene LibraryPolymerase Chain ReactionEpitope Mapping

Funding

  • Fonds Wetenschappelijk Onderzoek
Citations
759
FWCI
7.74
field-weighted impact
References
29
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98%
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References
By-passing immunization
Journal of Molecular Biology · 1991 · 1,599 citations
Making Antibodies by Phage Display Technology
Annual Review of Immunology · 1994 · 1,524 citations
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Selection and identification of single domain antibody fragments from camel heavy‐chain antibodies · Scinovex