Stöhr J, Condello C, Watts JC, Bloch L, Oehler A, Nick M, DeArmond SJ, Giles K, DeGrado WF, Prusiner SB. Distinct synthetic Aβ prion strains producing different amyloid deposits in bigenic mice. Proc Natl Acad Sci U S A. 2014 Jul 15;111(28):10329-34. Epub 2014 Jun 30 PubMed.

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  1. The prion paradigm has considerable explanatory power for the ontogeny of human neurodegenerative diseases, which mostly appear to emerge from the endogenous misfolding and seeded aggregation of disease-specific proteins. These two papers add to burgeoning evidence that disease-associated proteins can assume subtly different three-dimensional shapes, i.e. "strains," and that shape influences the pathogenic features of the resulting aggregates. Key findings of these studies are that it is possible to generate biologically active strains of aggregated Aβ from synthetic peptides, and that both synthetic and AD-derived abeta strains can be seeded and propagated in vivo. If strains are differentially sensitive to therapeutics, developing a universally effective intervention could be difficult. On the other hand, if disease-relevant, human-like Aβ strains can be generated in mouse models, the resulting mice might more effectively predict the efficacy of therapeutics and diagnostics in humans.

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  1. More Evidence Ties Aβ Strains to Distinct Pathologies