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Obtaining these MPs in a soluble and stable form constitutes a real challenge, regardless of the application purposes (e.g. quantification\/characterization assays, diagnosis, and preventive and curative strategies). A rapid process to obtain a native\u2010like antigen by solubilization of a full\u2010length MP directly from a pathogen is reported herein. Rabies virus (RABV) was used as a model for this demonstration and its full\u2010length G glycoprotein (RABV\u2010G) was stabilized with amphipathic polymers, named amphipols (APols). The stability of RABV\u2010G trapped in APol A8\u201035 (RABV\u2010G\/A8\u201035) was evaluated under different stress conditions (temperature, agitation, and light exposure). RABV\u2010G\/A8\u201035 in liquid form exhibited higher unfolding temperature (+6\u00b0C) than in detergent and was demonstrated to be antigenically stable over 1 month at 5\u00b0C and 25\u00b0C. Kinetic modeling of antigenicity data predicted antigenic stability of RABV\u2010G\/A8\u201035 in a solution of up to 1 year at 5\u00b0C. The RABV\u2010G\/A8\u201035 complex formulated in an optimized buffer composition and subsequently freeze\u2010dried displayed long\u2010term stability for 2\u2010years at 5, 25, and 37\u00b0C. This study reports for the first time that a natural full\u2010length MP extracted from a virus, complexed to APols and subsequently freeze\u2010dried, displayed long\u2010term antigenic stability, without requiring storage under refrigerated conditions.<\/jats:p>","DOI":"10.1002\/bit.27900","type":"journal-article","created":{"date-parts":[[2021,7,23]],"date-time":"2021-07-23T11:12:13Z","timestamp":1627038733000},"page":"4317-4330","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Full\u2010length G glycoprotein directly extracted from rabies virus with detergent and then stabilized by amphipols in liquid and freeze\u2010dried forms"],"prefix":"10.1002","volume":"118","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8395-9430","authenticated-orcid":false,"given":"Didier","family":"Cl\u00e9net","sequence":"first","affiliation":[{"name":"Bioprocess R&amp;D Department Sanofi Pasteur Marcy l'Etoile France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L\u00e9na","family":"Clavier","sequence":"additional","affiliation":[{"name":"Bioprocess R&amp;D Department Sanofi Pasteur Marcy l'Etoile France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beno\u00eet","family":"Strobbe","sequence":"additional","affiliation":[{"name":"Bioprocess R&amp;D Department Sanofi Pasteur Marcy l'Etoile France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christel","family":"Le Bon","sequence":"additional","affiliation":[{"name":"Laboratoire de Biologie Physico\u2010Chimique des Prot\u00e9ines Membranaires, CNRS, Institut de Biologie Physico\u2010Chimique Universit\u00e9 de Paris Paris France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2648-7868","authenticated-orcid":false,"given":"Manuela","family":"Zoonens","sequence":"additional","affiliation":[{"name":"Laboratoire de Biologie Physico\u2010Chimique des Prot\u00e9ines Membranaires, CNRS, Institut de Biologie Physico\u2010Chimique Universit\u00e9 de Paris Paris France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aure","family":"Saulnier","sequence":"additional","affiliation":[{"name":"Bioprocess R&amp;D Department Sanofi Pasteur Marcy l'Etoile France"},{"name":"Department of Analytical Sciences Sanofi Pasteur Marcy l'Etoile France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2021,8,5]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.1007\/s11095-006-9191-2"},{"key":"e_1_2_11_3_1","doi-asserted-by":"publisher","DOI":"10.3390\/v4010117"},{"key":"e_1_2_11_4_1","volume-title":"Membrane proteins can be solubilized and purified in detergents. in molecular biology of the cell","author":"Alberts B J. 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