Title |
Chimeric antigens displaying GPR65 extracellular loops on a soluble scaffold enabled the discovery of antibodies, which recognized native receptor
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Published in |
Bioengineered, January 2024
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DOI | 10.1080/21655979.2023.2299522 |
Pubmed ID | |
Authors |
Janine Barrett, Seppe Leysen, Cécile Galmiche, Hussein Al-Mossawi, Paul Bowness, Thomas E. Edwards, Alastair D.G. Lawson |
Abstract |
GPR65 is a proton-sensing G-protein coupled receptor associated with multiple immune-mediated inflammatory diseases, whose function is relatively poorly understood. With few reagents commercially available to probe the biology of receptor, generation of an anti-GPR65 monoclonal antibody was desired. Using soluble chimeric scaffolds, such as ApoE3, displaying the extracellular loops of GPR65, together with established phage display technology, native GPR65 loop-specific antibodies were identified. Phage-derived loop-binding antibodies recognized the wild-type native receptor to which they had not previously been exposed, generating confidence in the use of chimeric soluble proteins to act as efficient surrogates for membrane protein extracellular loop antigens. This technique provides promise for the rational design of chimeric antigens in facilitating the discovery of specific antibodies to GPCRs. |
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United States | 2 | 67% |
Unknown | 1 | 33% |
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Members of the public | 3 | 100% |
Mendeley readers
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Unknown | 2 | 100% |
Demographic breakdown
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Student > Ph. D. Student | 1 | 50% |
Professor > Associate Professor | 1 | 50% |
Readers by discipline | Count | As % |
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Biochemistry, Genetics and Molecular Biology | 1 | 50% |
Engineering | 1 | 50% |