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      Properties, production, and applications of camelid single-domain antibody fragments

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          Abstract

          Camelids produce functional antibodies devoid of light chains of which the single N-terminal domain is fully capable of antigen binding. These single-domain antibody fragments (VHHs or Nanobodies®) have several advantages for biotechnological applications. They are well expressed in microorganisms and have a high stability and solubility. Furthermore, they are well suited for construction of larger molecules and selection systems such as phage, yeast, or ribosome display. This minireview offers an overview of (1) their properties as compared to conventional antibodies, (2) their production in microorganisms, with a focus on yeasts, and (3) their therapeutic applications.

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

          M Arbabi Ghahroudi, A Desmyter, L Wyns … (1997)
          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.
          Article 0 comments Cited 206 times – based on 0 reviews     Review now
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            A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks.

            A S Greenberg, D. Avila, M. Hughes … (1995)
            Immunoglobulin and T-cell receptor (TCR) molecules are central to the adaptive immune system. Sequence conservation, similarities in domain structure, and usage of similar recombination signal sequences and recombination machinery indicate that there was probably a time during evolution when an ancestral receptor diverged to the modern-day immunoglobulin and TCR. Other molecules that undergo rearrangement have not been described in vertebrates, nor have intermediates been identified that have features of both these gene families. We report here the isolation of a new member of the immunoglobulin superfamily from the nurse shark, Ginglymostoma cirratum, which contains one variable and five constant domains and is found as a dimer in serum.
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              Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli.

              E Ward, D Güssow, A. D. Griffiths … (1989)
              In antibodies, a heavy and a light chain variable domain, VH and VL, respectively, pack together and the hypervariable loops on each domain contribute to binding antigen. We find, however, that isolated VH domains with good antigen-binding affinities can also be prepared. Using the polymerase chain reaction, diverse libraries of VH genes were cloned from the spleen genomic DNA of mice immunized with either lysozyme or keyhole-limpet haemocyanin. From these libraries, VH domains were expressed and secreted from Escherichia coli. Binding activities were detected against both antigens, and two VH domains were characterized with affinities for lysozyme in the 20 nM range. Isolated variable domains may offer an alternative to monoclonal antibodies and serve as the key to building high-affinity human antibodies. We suggest the name 'single domain antibodies (dAbs)' for these antigen binding demands.
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                Author and article information

                Contributors
                : +31-32-238436 , +31-32-238961 , michiel.harmsen@wur.nl
                Journal
                Journal ID (nlm-ta): Appl Microbiol Biotechnol
                Title: Applied Microbiology and Biotechnology
                Publisher: Springer-Verlag (Berlin/Heidelberg )
                ISSN (Print): 0175-7598
                ISSN (Electronic): 1432-0614
                Publication date (Electronic): 18 August 2007
                Publication date (Print): November 2007
                Volume: 77
                Issue: 1
                Pages: 13-22
                Affiliations
                [1 ]Institute for Animal Science and Health (ID-Lelystad) of Wageningen University and Research Centre, Edelhertweg 15, 8219 PH Lelystad, The Netherlands
                [2 ]Ablynx N.V., Technologiepark 4, 9052 Zwijnaarde, Belgium
                Article
                Publisher ID: 1142
                DOI: 10.1007/s00253-007-1142-2
                PMC ID: 2039825
                PubMed ID: 17704915
                SO-VID: 5320af28-91b3-444a-ac64-7ec6ac42e0e4
                Copyright © © Springer-Verlag 2007
                History
                Date received : 13 June 2007
                Date revision received : 25 July 2007
                Date accepted : 30 July 2007
                Categories
                Subject: Mini-Review
                Custom metadata
                issue-copyright-statement © Springer-Verlag 2007

                ScienceOpen disciplines: Biotechnology
                Keywords: glycosylation,yeast,microbial production,single-domain
                Data availability:
                ScienceOpen disciplines: Biotechnology
                Keywords: glycosylation, yeast, microbial production, single-domain

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