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Antibodies (Basel). 2016 May 02;5(2). doi: 10.3390/antib5020011.

Generating Recombinant Antibodies to Membrane Proteins through Phage Display.

Antibodies (Basel, Switzerland)

Renhua Huang, Margaret M Kiss, Melissa Batonick, Michael P Weiner, Brian K Kay

Affiliations

  1. Department of Biological Sciences, University of Illinois at Chicago, Chicago, IL 60607-7060, USA. [email protected].
  2. AxioMx Inc., a subsidiary of Abcam Plc, Branford, CT 06405, USA. [email protected].
  3. AxioMx Inc., a subsidiary of Abcam Plc, Branford, CT 06405, USA. [email protected].
  4. AxioMx Inc., a subsidiary of Abcam Plc, Branford, CT 06405, USA. [email protected].
  5. Department of Biological Sciences, University of Illinois at Chicago, Chicago, IL 60607-7060, USA. [email protected].

PMID: 31557992 PMCID: PMC6698964 DOI: 10.3390/antib5020011

Abstract

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.

Keywords: G-protein coupled receptors (GPCRs); affinity selection; fragments of antigen binding (Fabs); membrane proteins; nanodiscs; phage-display; recombinant antibodies; single-domain antibodies; transfection; virus-like particles (VLPs)

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