Prion Protein Amino Acid Determinants of Differential Susceptibility and Molecular Feature of Prion Strains in Mice and Voles

Bank vole Gerbil Vole Arvicolinae Weasel
DOI: 10.1371/journal.ppat.1000113 Publication Date: 2008-07-24T22:18:26Z
ABSTRACT
The bank vole is a rodent susceptible to different prion strains from humans and various animal species. We analyzed the transmission features of prions in panel seven species which showed degrees phylogenetic affinity specific protein (PrP) sequence divergences order investigate basis susceptibility comparison other models. At first, we found differential field voles compared C57Bl/6 wood mice. Voles high sheep scrapie but were resistant bovine spongiform encephalopathy, whereas mice displayed opposite features. Infection with mouse-adapted 139A was faster than Moreover, glycoprofile change observed voles, reverted upon back passage All replicated much after adapting new PrP indicated correlation between patterns amino acids at positions 154 169 (Y S mice, N voles). This confirmed when inoculating three additional species: gerbils, spiny oldfield 139A. These rodents chosen because do have 154N 169N substitutions, gerbil not them. Our results suggest that residues drive susceptibility, molecular phenotype replication rate rodents. might implications for assessment host range traceability strains, as well development improved models diseases.
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