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Properties, Production, and Applications of Camelid Single-domain Antibody Fragments

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Date 2007 Aug 21
PMID 17704915
Citations 289
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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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References
1.
Rothbauer U, Zolghadr K, Tillib S, Nowak D, Schermelleh L, Gahl A . Targeting and tracing antigens in live cells with fluorescent nanobodies. Nat Methods. 2006; 3(11):887-9. DOI: 10.1038/nmeth953. View

2.
Davies J, Riechmann L . Single antibody domains as small recognition units: design and in vitro antigen selection of camelized, human VH domains with improved protein stability. Protein Eng. 1996; 9(6):531-7. DOI: 10.1093/protein/9.6.531. View

3.
Whitlow M, Bell B, Feng S, Filpula D, HARDMAN K, Hubert S . An improved linker for single-chain Fv with reduced aggregation and enhanced proteolytic stability. Protein Eng. 1993; 6(8):989-95. DOI: 10.1093/protein/6.8.989. View

4.
Streltsov V, Varghese J, Carmichael J, Irving R, Hudson P, Nuttall S . Structural evidence for evolution of shark Ig new antigen receptor variable domain antibodies from a cell-surface receptor. Proc Natl Acad Sci U S A. 2004; 101(34):12444-9. PMC: 515081. DOI: 10.1073/pnas.0403509101. View

5.
De Genst E, Silence K, Decanniere K, Conrath K, Loris R, Kinne J . Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies. Proc Natl Acad Sci U S A. 2006; 103(12):4586-91. PMC: 1450215. DOI: 10.1073/pnas.0505379103. View