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Review
. 2007 Nov;77(1):13-22.
doi: 10.1007/s00253-007-1142-2. Epub 2007 Aug 18.

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

Affiliations
Review

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

M M Harmsen et al. Appl Microbiol Biotechnol. 2007 Nov.

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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Figures

Fig. 1
Fig. 1
Schematic diagram of conventional (a) and heavy-chain (b) antibodies and fragments thereof. Variable domains derived from the antibody heavy (VH) and light (VL) chains are shaded dark gray and light gray, respectively, whereas constant domains (CH and CL) are not shaded. Note the absence of the light chain and CH1 domain in heavy-chain antibodies. Antibody domains that pair by noncovalent interactions are indicated by overlaying them. The B-subunits of naturally pentamerizing toxins that are used to generate pentabodies are indicated as hatched spheres

References

    1. Alvarez-Rueda N, Behar G, Ferre V, Pugniere M, Roquet F, Gastinel L, Jacquot C, Aubry J, Baty D, Barbet J, Birkle S. Generation of llama single-domain antibodies against methotrexate, a prototypical hapten. Mol Immunol. 2007;44:1680–1690. - PubMed
    1. Arbabi-Ghahroudi M, Desmyter A, Wyns L, Hamers R, Muyldermans S. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 1997;414:521–526. - PubMed
    1. Arbabi-Ghahroudi M, Tanha J, MacKenzie R. Prokaryotic expression of antibodies. Cancer Metastasis Rev. 2005;24:501–519. - PubMed
    1. Baral TN, Magez S, Stijlemans B, Conrath K, Vanhollebeke B, Pays E, Muyldermans S, De Baetselier P. Experimental therapy of African trypanosomiasis with a nanobody-conjugated human trypanolytic factor. Nat Med. 2006;12:580–584. - PubMed
    1. Bond CJ, Marsters JC, Sidhu SS. Contributions of CDR3 to VHH domain stability and the design of monobody scaffolds for naive antibody libraries. J Mol Biol. 2003;332:643–655. - PubMed

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