Prion Strain Interactions Are Highly Selective
2010 (English)In: JOURNAL OF NEUROSCIENCE, ISSN 0270-6474, Vol. 30, no 36, 12094-12102 p.Article in journal (Refereed) Published
Various misfolded and aggregated neuronal proteins commonly coexist in neurodegenerative disease, but whether the proteins coaggregate and alter the disease pathogenesis is unclear. Here we used mixtures of distinct prion strains, which are believed to differ in conformation, to test the hypothesis that two different aggregates interact and change the disease in vivo. We tracked two prion strains in mice histopathologically and biochemically, as well as by spectral analysis of plaque-bound PTAA (polythiophene acetic acid), a conformation-sensitive fluorescent amyloid ligand. We found that prion strains interacted in a highly selective and strain-specific manner, with (1) no interaction, (2) hybrid plaque formation, or (3) blockage of one strain by a second (interference). The hybrid plaques were maintained on additional passage in vivo and each strain seemed to maintain its original conformational properties, suggesting that one strain served only as a scaffold for aggregation of the second strain. These findings not only further our understanding of prion strain interactions but also directly demonstrate interactions that may occur in other protein aggregate mixtures.
Place, publisher, year, edition, pages
Society for Neuroscience , 2010. Vol. 30, no 36, 12094-12102 p.
Engineering and Technology
IdentifiersURN: urn:nbn:se:liu:diva-60699DOI: 10.1523/JNEUROSCI.2417-10.2010ISI: 000281768000021OAI: oai:DiVA.org:liu-60699DiVA: diva2:359868
Original Publication: Peter Nilsson, Shivanjali Joshi-Barr, Olivia Winson and Christina J Sigurdson, Prion Strain Interactions Are Highly Selective, 2010, JOURNAL OF NEUROSCIENCE, (30), 36, 12094-12102. http://dx.doi.org/10.1523/JNEUROSCI.2417-10.2010 Copyright: Society for Neuroscience http://www.sfn.org/2010-11-012010-10-222015-05-28