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

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 a...

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Detalles Bibliográficos
Autores principales: Harmsen, M. M., De Haard, H. J.
Formato: Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2007
Materias:
Mini-Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2039825/
https://www.ncbi.nlm.nih.gov/pubmed/17704915
http://dx.doi.org/10.1007/s00253-007-1142-2
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author Harmsen, M. M.
De Haard, H. J.
author_facet Harmsen, M. M.
De Haard, H. J.
author_sort Harmsen, M. M.
collection PubMed
description 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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spelling pubmed-20398252007-10-29 Properties, production, and applications of camelid single-domain antibody fragments Harmsen, M. M. De Haard, H. J. Appl Microbiol Biotechnol Mini-Review 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. Springer Berlin Heidelberg 2007-08-18 2007 /pmc/articles/PMC2039825/ /pubmed/17704915 http://dx.doi.org/10.1007/s00253-007-1142-2 Text en © Springer-Verlag 2007 This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Mini-Review
Harmsen, M. M.
De Haard, H. J.
Properties, production, and applications of camelid single-domain antibody fragments
title Properties, production, and applications of camelid single-domain antibody fragments
title_full Properties, production, and applications of camelid single-domain antibody fragments
title_fullStr Properties, production, and applications of camelid single-domain antibody fragments
title_full_unstemmed Properties, production, and applications of camelid single-domain antibody fragments
title_short Properties, production, and applications of camelid single-domain antibody fragments
title_sort properties, production, and applications of camelid single-domain antibody fragments
topic Mini-Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2039825/
https://www.ncbi.nlm.nih.gov/pubmed/17704915
http://dx.doi.org/10.1007/s00253-007-1142-2
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