A size threshold limits prion transmission and establishes phenotypic diversity

Aaron Derdowski, Suzanne S. Sindi, Courtney L. Klaips, Susanne DiSalvo, Tricia R. Serio

Research output: Contribution to journalArticlepeer-review

85 Scopus citations


According to the prion hypothesis, atypical phenotypes arise when a prion protein adopts an alternative conformation and persist when that form assembles into self-replicating aggregates. Amyloid formation in vitro provides a model for this protein-misfolding pathway, but the mechanism by which this process interacts with the cellular environment to produce transmissible phenotypes is poorly understood. Using the yeast prion Sup35/[PSI+], we found that protein conformation determined the size distribution of aggregates through its interactions with a molecular chaperone. Shifts in this range created variations in aggregate abundance among cells because of a size threshold for transmission, and this heterogeneity, along with aggregate growth and fragmentation, induced age-dependent fluctuations in phenotype. Thus, prion conformations may specify phenotypes as population averages in a dynamic system.

Original languageEnglish (US)
Pages (from-to)680-683
Number of pages4
Issue number6004
StatePublished - Oct 29 2010

ASJC Scopus subject areas

  • General


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