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

By M. Harmsen, H. de Haard. Applied Microbiology and Biotechnology, 2007

793 citations recorded by the source corpus.

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.

Subfields: Biotechnology, Molecular Biology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/3c09f1b90fbfd8f2dabf1e6741267dbe8bffde50

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In Molecular Biology

1. Menči Kunstelj
2. Vladka Gaberc Porekar
3. S. Jevševar

In Radiology, Nuclear Medicine and Imaging

1. Menči Kunstelj
2. Vladka Gaberc Porekar
3. S. Jevševar

Citations in the corpus

• PEGylation of therapeutic proteins (2010, background): “An example of a successful application of PEGylation to nanobodies is the PEGylated nanobody neutralizing foot and mouth disease (FMD) virus [15].”