Quiescin-sulfhydryl oxidase inhibits prion formation in vitro
| العنوان: | Quiescin-sulfhydryl oxidase inhibits prion formation in vitro |
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| المؤلفون: | Yu Li, Johnny Dang, Li Cui, Zerui Wang, Liang Zeng, Robert B. Petersen, Qingzhong Kong, Jue Yuan, Sylvain Lehmann, Jacqueline Mikol, Manuel Camacho Martinez, Romany Abskharon, Alexandre Wohlkonig, Yi An Zhan, Gong Xiang Wang, Shizhong Bu, Jan Steyaert, Wen-Quan Zou |
| المساهمون: | Structural Biology Brussels, Department of Bio-engineering Sciences, Service d'anatomie et cytologie pathologiques, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Lariboisière-Fernand-Widal [APHP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Diderot - Paris 7 (UPD7), Cellules Souches, Plasticité Cellulaire, Médecine Régénératrice et Immunothérapies (IRMB), Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier), Université Paris Diderot - Paris 7 (UPD7)-Hôpital Lariboisière-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP), Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Assistance publique - Hôpitaux de Paris (AP-HP)-Hôpital Lariboisière-Université Paris Diderot - Paris 7 ( UPD7 ), CHU Saint-Eloi-Centre Hospitalier Régional Universitaire [Montpellier] ( CHRU Montpellier ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université de Montpellier ( UM ) |
| المصدر: | Aging Aging, Impact Journals, 2016, 8 (12), pp.3419-3429. ⟨10.18632/aging.101132⟩ Aging, Superintendent of Documents, U.S. Government Printing Office, 2016, 8 (12), pp.3419-3429. ⟨10.18632/aging.101132⟩ Aging, Superintendent of Documents, U.S. Government Printing Office, 2016, 8 (12), pp.3419-3429. 〈10.18632/aging.101132〉 |
| بيانات النشر: | Impact Journals, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0301 basic medicine, Gene isoform, Aging, animal diseases, Scrapie, scrapie-infected mouse neuroblastoma cells (ScN2a), [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, law.invention, 03 medical and health sciences, law, protein misfolding cyclic amplification, recombinant prion protein, Histone octamer, prions, Quiescin sulfhydryl oxidase (QSOX), Oxidase test, 030102 biochemistry & molecular biology, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, Cell Biology, Molecular biology, In vitro, 3. Good health, nervous system diseases, 030104 developmental biology, Recombinant DNA, Protein Misfolding Cyclic Amplification, Protein folding |
| الوصف: | International audience; Prions are infectious proteins that cause a group of fatal transmissible diseases in animals and humans. The scrapie isoform (PrPSc) of the cellular prion protein (PrPC) is the only known component of the prion. Several lines of evidence have suggested that the formation and molecular features of PrPSc are associated with an abnormal unfolding/refolding process. Quiescin-sulfhydryl oxidase (QSOX) plays a role in protein folding by introducing disulfides into unfolded reduced proteins. Here we report that QSOX inhibits human prion propagation in protein misfolding cyclic amplification reactions and murine prion propagation in scrapie-infected neuroblastoma cells. Moreover, QSOX preferentially binds PrPSc from prion-infected human or animal brains, but not PrPC from uninfected brains. Surface plasmon resonance of the recombinant mouse PrP (moPrP) demonstrates that the affinity of QSOX for monomer is significantly lower than that for octamer (312 nM vs 1.7 nM). QSOX exhibits much lower affinity for N-terminally truncated moPrP (PrP89-230) than for the full-length moPrP (PrP23-231) (312 nM vs 2 nM), suggesting that the N-terminal region of PrP is critical for the interaction of PrP with QSOX. Our study indicates that QSOX may play a role in prion formation, which may open new therapeutic avenues for treating prion diseases. |
| اللغة: | English |
| تدمد: | 1945-4589 0002-0966 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14c30d722c4c61271836b3b842a3a530Test https://biblio.vub.ac.be/vubir/quiescinsulfhydryl-oxidase-inhibits-prion-formation-in-vitroTest(976ea05e-5aa5-43b3-acd1-8ac2f53e985d).html |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....14c30d722c4c61271836b3b842a3a530 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19454589 00020966 |
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