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Application of an in vitro-amplification assay as a novel pre-screening test for compounds inhibiting the aggregation of prion protein scrapie.
Schmitz, Matthias; Cramm, Maria; Llorens, Franc; Candelise, Niccolò; Müller-Cramm, Dominik; Varges, Daniela; Schulz-Schaeffer, Walter J; Zafar, Saima; Zerr, Inga.
Afiliación
  • Schmitz M; Department of Neurology, University Medical Center Göttingen and German Center for Neurodegenerative Diseases (DZNE)-Göttingen campus, Göttingen, Germany.
  • Cramm M; Department of Neurology, University Medical Center Göttingen and German Center for Neurodegenerative Diseases (DZNE)-Göttingen campus, Göttingen, Germany.
  • Llorens F; Department of Neurology, University Medical Center Göttingen and German Center for Neurodegenerative Diseases (DZNE)-Göttingen campus, Göttingen, Germany.
  • Candelise N; Department of Neurology, University Medical Center Göttingen and German Center for Neurodegenerative Diseases (DZNE)-Göttingen campus, Göttingen, Germany.
  • Müller-Cramm D; Department of Neurology, University Medical Center Göttingen and German Center for Neurodegenerative Diseases (DZNE)-Göttingen campus, Göttingen, Germany.
  • Varges D; Department of Neurology, University Medical Center Göttingen and German Center for Neurodegenerative Diseases (DZNE)-Göttingen campus, Göttingen, Germany.
  • Schulz-Schaeffer WJ; Department of Neuropathology, Georg-August University, 37075 Göttingen, Germany.
  • Zafar S; Department of Neurology, University Medical Center Göttingen and German Center for Neurodegenerative Diseases (DZNE)-Göttingen campus, Göttingen, Germany.
  • Zerr I; Department of Neurology, University Medical Center Göttingen and German Center for Neurodegenerative Diseases (DZNE)-Göttingen campus, Göttingen, Germany.
Sci Rep ; 6: 28711, 2016 07 07.
Article en En | MEDLINE | ID: mdl-27385410
In vitro amplification assays, such as real-time quaking-induced conversion (RT-QuIC) are used to detect aggregation activity of misfolded prion protein (PrP) in brain, cerebrospinal fluid (CSF) and urine samples from patients with a prion disease. We believe that the method also has a much broader application spectrum. In the present study, we applied RT-QuIC as a pre-screening test for substances that potentially inhibit the aggregation process of the cellular PrP (PrP(C)) to proteinase (PK)-resistant PrP(res). We chose doxycycline as the test substance as it has been tested successfully in animal models and proposed in clinical studies as a therapeutic for prion diseases. The RT-QuIC-reaction was seeded with brain tissue or CSF from sCJD patients and doxycycline was then added in different concentrations as well as at different time points. In both experiments, we observed a dose- and time-dependent inhibition of the RT-QuIC seeding response and a decrease of PK resistant PrP(res) when doxycycline was added. In contrast, ampicillin or sucrose had no effect on the RT-QuIC seeding response. Our study is the first to apply RT-QuIC as a pre-screening assay for compounds inhibiting the PrP aggregation in vitro and confirms that doxycycline is an efficient inhibitor of the PrP aggregation process in RT-QuIC analysis.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Síndrome de Creutzfeldt-Jakob / Proteínas Priónicas Tipo de estudio: Diagnostic_studies / Prognostic_studies / Screening_studies Límite: Animals / Humans Idioma: En Revista: Sci Rep Año: 2016 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Síndrome de Creutzfeldt-Jakob / Proteínas Priónicas Tipo de estudio: Diagnostic_studies / Prognostic_studies / Screening_studies Límite: Animals / Humans Idioma: En Revista: Sci Rep Año: 2016 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido