期刊
VIROLOGY
卷 379, 期 2, 页码 284-293出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2008.07.006
关键词
protein aggregation; PrP; PrP-res; PrP-sen; prion; scrapie; transmissible spongiform encephalopathy; TSE
类别
资金
- University of Montana Department of Biomedical and Pharmaceutical Sciences Neuroscience program
- NIH, National Institute of Allergy and Infectious Diseases [1-Z01-AI000752-12]
- NIH [R01 NS040975]
Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases that include Creutzfeldt-Jakob disease, bovine spongiform encephalopathy and sheep scrapie. Although one of the earliest events during TSE infection is the cellular uptake of protease resistant prion protein (PrP-res), this process is poorly understood due to the difficulty of clearly distinguishing input PrP-res from either PrP-res or protease-sensitive PrP (PrP-sen) made by the cell. Using PrP-res tagged with a unique antibody epitope, we examined PrP-res uptake in neuronal and fibroblast cells exposed to three different mouse scrapie strains. Pi-P-res uptake was rapid and independent of scrapie strain, cell type, or cellular PrP expression, but occurred in only a subset of cells and was influenced by PrP-res preparation and aggregate size. Our results suggest that Pi-P-res aggregate size, the PrP-res microenvironment, and/or host cell-specific factors can all influence whether or not a cell takes up PrP-res following exposure to TSE infectivity. (C) 2008 Elsevier Inc. All rights reserved.
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