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In vitro nanobody discovery for integral membrane protein targets
Nanobodies (Nbs) or single-domain antibodies are among the smallest and most stable binder scaffolds known. In vitro display is a powerful antibody discovery technique used worldwide. We describe the first adaptation of in vitro mRNA/cDNA display for the rapid, automatable discovery of Nbs against d...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4208029/ https://www.ncbi.nlm.nih.gov/pubmed/25342225 http://dx.doi.org/10.1038/srep06760 |
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author | Doshi, Rupak Chen, Beverly R. Vibat, Cecile Rose T. Huang, Norman Lee, Chang-Wook Chang, Geoffrey |
author_facet | Doshi, Rupak Chen, Beverly R. Vibat, Cecile Rose T. Huang, Norman Lee, Chang-Wook Chang, Geoffrey |
author_sort | Doshi, Rupak |
collection | PubMed |
description | Nanobodies (Nbs) or single-domain antibodies are among the smallest and most stable binder scaffolds known. In vitro display is a powerful antibody discovery technique used worldwide. We describe the first adaptation of in vitro mRNA/cDNA display for the rapid, automatable discovery of Nbs against desired targets, and use it to discover the first ever reported nanobody against the human full-length glucose transporter, GLUT-1. We envision our streamlined method as a bench-top platform technology, in combination with various molecular evolution techniques, for expedited Nb discovery. |
format | Online Article Text |
id | pubmed-4208029 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-42080292014-10-27 In vitro nanobody discovery for integral membrane protein targets Doshi, Rupak Chen, Beverly R. Vibat, Cecile Rose T. Huang, Norman Lee, Chang-Wook Chang, Geoffrey Sci Rep Article Nanobodies (Nbs) or single-domain antibodies are among the smallest and most stable binder scaffolds known. In vitro display is a powerful antibody discovery technique used worldwide. We describe the first adaptation of in vitro mRNA/cDNA display for the rapid, automatable discovery of Nbs against desired targets, and use it to discover the first ever reported nanobody against the human full-length glucose transporter, GLUT-1. We envision our streamlined method as a bench-top platform technology, in combination with various molecular evolution techniques, for expedited Nb discovery. Nature Publishing Group 2014-10-24 /pmc/articles/PMC4208029/ /pubmed/25342225 http://dx.doi.org/10.1038/srep06760 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-nd/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/ |
spellingShingle | Article Doshi, Rupak Chen, Beverly R. Vibat, Cecile Rose T. Huang, Norman Lee, Chang-Wook Chang, Geoffrey In vitro nanobody discovery for integral membrane protein targets |
title | In vitro nanobody discovery for integral membrane protein targets |
title_full | In vitro nanobody discovery for integral membrane protein targets |
title_fullStr | In vitro nanobody discovery for integral membrane protein targets |
title_full_unstemmed | In vitro nanobody discovery for integral membrane protein targets |
title_short | In vitro nanobody discovery for integral membrane protein targets |
title_sort | in vitro nanobody discovery for integral membrane protein targets |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4208029/ https://www.ncbi.nlm.nih.gov/pubmed/25342225 http://dx.doi.org/10.1038/srep06760 |
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