title: Strain conformation controls the specificity of cross-species prion transmission in the yeast model.
abstract: Transmissible self-assembled fibrous cross-β polymer infectious proteins (prions) cause neurodegenerative diseases in mammals and control non-Mendelian heritable traits in yeast. Cross-species prion transmission is frequently impaired, due to sequence differences in prion-forming proteins. Recent studies of prion species barrier on the model of closely related yeast species show that colocalization of divergent proteins is not sufficient for the cross-species prion transmission, and that an identity of specific amino acid sequences and a type of prion conformational variant (strain) play a major role in the control of transmission specificity. In contrast, chemical compounds primarily influence transmission specificity via favoring certain strain conformations, while the species origin of the host cell has only a relatively minor input. Strain alterations may occur during cross-species prion conversion in some combinations. The model is discussed which suggests that different recipient proteins can acquire different spectra of prion strain conformations, which could be either compatible or incompatible with a particular donor strain.
authors: a Laboratory of Amyloid Biology, St. Petersburg State University , St. Petersburg , Russia.|b Institute of Translational Biomedicine, St. Petersburg State University , St. Petersburg , Russia.|c Department of Genetics and Biotechnology , St. Petersburg State University , St. Petersburg , Russia.
authors: Anastasia V
authors: AV
authors: Grizel
authors: a Laboratory of Amyloid Biology, St. Petersburg State University , St. Petersburg , Russia.|b Institute of Translational Biomedicine, St. Petersburg State University , St. Petersburg , Russia.|c Department of Genetics and Biotechnology , St. Petersburg State University , St. Petersburg , Russia.
authors: Aleksandr A
authors: AA
authors: Rubel
authors: a Laboratory of Amyloid Biology, St. Petersburg State University , St. Petersburg , Russia.|b Institute of Translational Biomedicine, St. Petersburg State University , St. Petersburg , Russia.|d School of Biological Sciences, Georgia Institute of Technology , Atlanta , GA , USA.
authors: Yury O
authors: YO
authors: Chernoff
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D008954:Models, Biological; D011328:Prions / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D012440:Saccharomyces / Q000145:classification* / Q000254:growth & development / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D013045:Species Specificity
chemical_list: D000682:Amyloid; D011328:Prions; D029701:Saccharomyces cerevisiae Proteins
keywords: Saccharomyces cerevisiae; Saccharomyces paradoxus; Saccharomyces uvarum; Sup35; [PSI+]; amyloid; prion variant