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Chemical and biophysical insights into the propagation of prion strains
Institute of Neuropathology, Zurich.
Linköping University, Department of Physics, Chemistry and Biology, Organic Chemistry. Linköping University, The Institute of Technology.ORCID iD: 0000-0002-5582-140X
University of Cambridge.
Institute of Neuropathology, Zurich.
2008 (English)In: HFSP JOURNAL, ISSN 1955-2068, Vol. 2, no 6, 332-341 p.Article in journal (Refereed) Published
Abstract [en]

Transmissible spongiform encephalopathies (TSEs) are lethal infectious neurodegenerative diseases. TSEs are caused by prions, infectious agents lacking informational nucleic acids, and possibly identical with higher-order aggregates of the cellular glycolipoprotein PrPC. Prion strains are derived from TSE isolates that, even after inoculation into genetically identical hosts, cause disease with distinct patterns of protein aggregate deposition, incubation times, morphology of the characteristic brain damage, and cellular tropism. Most of these traits are relatively stable across serial passages. Here we review current techniques for studying prion strain differences in vivo and in cells, and discuss the strain phenomena in the general context of the knowledge gained from modeling prion fibril growth in vitro and in simple organisms.

Place, publisher, year, edition, pages
2008. Vol. 2, no 6, 332-341 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-16222DOI: 10.2976/1.2990786OAI: diva2:133467
Available from: 2009-01-12 Created: 2009-01-09 Last updated: 2014-04-08

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Nilsson, Peter
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