ArticleThe Journal of biological chemistry2016
Contributions of the Prion Protein Sequence, Strain, and Environment to the Species Barrier.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 47 citations in OpenAlex.
- Review
- Prion protein gene (PRNP) variation in German and Danish cervids.Veterinary research · 2024Article
- Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.Angewandte Chemie (International ed. in English) · 2023Article
- Decreased Water Mobility Contributes To Increased α-Synuclein Aggregation.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Multipotent antioxidant and antitoxicant potentiality of an indigenous probioticJournal of food science and technology · 2021Article
- Cervid Prion Protein Polymorphisms: Role in Chronic Wasting Disease Pathogenesis.International journal of molecular sciences · 2021Review
- α-Synuclein modulates tau spreading in mouse brains.The Journal of experimental medicine · 2021Article
- Familial globular glial tauopathy linked to MAPT mutations: molecular neuropathology and seeding capacity of a prototypical mixed neuronal and glial tauopathy.Acta neuropathologica · 2020Article
- Relevance of host tau in tau seeding and spreading in tauopathies.Brain pathology (Zurich, Switzerland) · 2020Article
- Article
- Challenges and Advances in Antemortem Diagnosis of Human Transmissible Spongiform Encephalopathies.Frontiers in bioengineering and biotechnology · 2020Review
- Targeted Forward Genetics: Population-Scale Analyses of Allele Replacements Spanning Thousands of Base Pairs in Fission Yeast.G3 (Bethesda, Md.) · 2019Article
- Biomolecular Assemblies: Moving from Observation to Predictive Design.Chemical reviews · 2018Review
- Seeding and cross-seeding fibrillation of N-terminal prion protein peptides PrP(120-144).Protein science : a publication of the Protein Society · 2018Article
- Modulation of the Formation of Aβ- and Sup35NM-Based Amyloids by Complex Interplay of Specific and Nonspecific Ion Effects.The journal of physical chemistry. B · 2018Article
- Differential effects of divalent cations on elk prion protein fibril formation and stability.Prion · 2018Article
- Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism.F1000Research · 2017Review
- Strain conformation controls the specificity of cross-species prion transmission in the yeast model.Prion · 2016Article
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid propagation requires high levels of sequence specificity so that only molecules with very high sequence identity can form cross-β-sheet structures of sufficient stringency for incorporation into the amyloid fibril. This sequence specificity presents a barrier to the transmission of prions between two species with divergent sequences, termed a species barrier. Here we study the relative effects of protein sequence, seed conformation, and environment on the species barrier strength and specificity for the yeast prion protein Sup35p from three closely related species of the Saccharomyces sensu stricto group; namely, Saccharomyces cerevisiae, Saccharomyces bayanus, and Saccharomyces paradoxus. Through in vivo plasmid shuffle experiments, we show that the major characteristics of the transmission barrier and conformational fidelity are determined by the protein sequence rather than by the cellular environment. In vitro data confirm that the kinetics and structural preferences of aggregation of the S. paradoxus and S. bayanus proteins are influenced by anions in accordance with their positions in the Hofmeister series, as observed previously for S. cerevisiae. However, the specificity of the species barrier is primarily affected by the sequence and the type of anion present during the formation of the initial seed, whereas anions present during the seeded aggregation process typically influence kinetics rather than the specificity of prion conversion. Therefore, our work shows that the protein sequence and the conformation variant (strain) of the prion seed are the primary determinants of cross-species prion specificity both in vivo and in vitro.
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