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

Applied Microbiology and Biotechnology · 2007 · Vol. 77(1) · pp. 13–22
Michiel M. HarmsenHans J. de Haard

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.

Monoclonal and Polyclonal Antibodies ResearchTransgenic Plants and ApplicationsGlycosylation and Glycoproteins ResearchSingle-domain antibodyPhage displayAntibodyYeastComputational biologyBiologyMicroorganismProtein engineeringChemistryBiochemistry

MeSH terms

AnimalsCamelids, New WorldImmunoglobulin FragmentsImmunoglobulin Heavy ChainsModels, Biological
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Cited by
Nanobodies: Natural Single-Domain Antibodies
Annual Review of Biochemistry · 2013 · 2,223 citations
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