Potential approaches for heterologous prion protein treatment of prion diseases
| Autor: | Pamela J. Skinner, Davis M. Seelig, Patricia A. Goodman |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
PrPSc Proteins medicine.medical_treatment animal diseases Hamster Heterologous Peptide Scrapie Disease Kaplan-Meier Estimate Biology Biochemistry law.invention prion 03 medical and health sciences Cellular and Molecular Neuroscience Mice law Cricetinae medicine Animals chemistry.chemical_classification Extra Views Protease treatment PrPC Cell Biology heterologous prion proteins Virology Recombinant Proteins nervous system diseases 030104 developmental biology Infectious Diseases chemistry Recombinant DNA Rabbits PrPres |
| Zdroj: | Prion |
| ISSN: | 1933-690X 1933-6896 |
| Popis: | Prion diseases, or transmissible spongiform encephalopathies (TSEs) are progressive, fatal neurodegenerative diseases with no effective treatment. The pathology of these diseases involves the conversion of a protease sensitive form of the cellular prion protein (PrPC) into a protease resistant infectious form (PrPres). The efficiency of this conversion is predicated upon a number of factors, most notably a strong homology between cellular PrPC and PrPres. In our recently published study, we infected mice with the RML-Chandler strain of scrapie and treated them with heterologous hamster prion proteins. This treatment was seen to reduce clinical signs of prion disease, to delay the onset of clinical symptoms and to prolong survival. In this current article we discuss potential mechanisms of action of treatment with heterologous prion proteins. We also discuss potential extensions of these studies using a heterologous rabbit PrP-based treatment strategy or a peptide based strategy, and improvement of treatment delivery including a lentiviral-based system. |
| Databáze: | OpenAIRE |
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