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Generating Recombinant Antibodies to Membrane Proteins through Phage Display

One of the most important classes of proteins in terms of drug targets is cell surface membrane proteins, and yet it is a challenging set of proteins for generating high-quality affinity reagents. In this review, we focus on the use of phage libraries, which display antibody fragments, for generatin...

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Autores principales: Huang, Renhua, Kiss, Margaret M., Batonick, Melissa, Weiner, Michael P., Kay, Brian K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6698964/
https://www.ncbi.nlm.nih.gov/pubmed/31557992
http://dx.doi.org/10.3390/antib5020011
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author Huang, Renhua
Kiss, Margaret M.
Batonick, Melissa
Weiner, Michael P.
Kay, Brian K.
author_facet Huang, Renhua
Kiss, Margaret M.
Batonick, Melissa
Weiner, Michael P.
Kay, Brian K.
author_sort Huang, Renhua
collection PubMed
description One of the most important classes of proteins in terms of drug targets is cell surface membrane proteins, and yet it is a challenging set of proteins for generating high-quality affinity reagents. In this review, we focus on the use of phage libraries, which display antibody fragments, for generating recombinant antibodies to membrane proteins. Such affinity reagents generally have high specificity and affinity for their targets. They have been used for cell staining, for promoting protein crystallization to solve three-dimensional structures, for diagnostics, and for treating diseases as therapeutics. We cover publications on this topic from the past 10 years, with a focus on the various formats of membrane proteins for affinity selection and the diverse affinity selection strategies used. Lastly, we discuss the challenges faced in this field and provide possible directions for future efforts.
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spelling pubmed-66989642019-09-05 Generating Recombinant Antibodies to Membrane Proteins through Phage Display Huang, Renhua Kiss, Margaret M. Batonick, Melissa Weiner, Michael P. Kay, Brian K. Antibodies (Basel) Review One of the most important classes of proteins in terms of drug targets is cell surface membrane proteins, and yet it is a challenging set of proteins for generating high-quality affinity reagents. In this review, we focus on the use of phage libraries, which display antibody fragments, for generating recombinant antibodies to membrane proteins. Such affinity reagents generally have high specificity and affinity for their targets. They have been used for cell staining, for promoting protein crystallization to solve three-dimensional structures, for diagnostics, and for treating diseases as therapeutics. We cover publications on this topic from the past 10 years, with a focus on the various formats of membrane proteins for affinity selection and the diverse affinity selection strategies used. Lastly, we discuss the challenges faced in this field and provide possible directions for future efforts. MDPI 2016-05-02 /pmc/articles/PMC6698964/ /pubmed/31557992 http://dx.doi.org/10.3390/antib5020011 Text en © 2016 by the authors Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Huang, Renhua
Kiss, Margaret M.
Batonick, Melissa
Weiner, Michael P.
Kay, Brian K.
Generating Recombinant Antibodies to Membrane Proteins through Phage Display
title Generating Recombinant Antibodies to Membrane Proteins through Phage Display
title_full Generating Recombinant Antibodies to Membrane Proteins through Phage Display
title_fullStr Generating Recombinant Antibodies to Membrane Proteins through Phage Display
title_full_unstemmed Generating Recombinant Antibodies to Membrane Proteins through Phage Display
title_short Generating Recombinant Antibodies to Membrane Proteins through Phage Display
title_sort generating recombinant antibodies to membrane proteins through phage display
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6698964/
https://www.ncbi.nlm.nih.gov/pubmed/31557992
http://dx.doi.org/10.3390/antib5020011
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