X-ray structural and molecular dynamical studies of the globular domains of cow, deer, elk and Syrian hamster prion proteins

Journal of Structural Biology
Pravas Kumar BaralMichael N G James

Abstract

Misfolded prion proteins are the cause of neurodegenerative diseases that affect many mammalian species, including humans. Transmission of the prion diseases poses a considerable public-health risk as a specific prion disease such as bovine spongiform encephalopathy can be transferred to humans and other mammalian species upon contaminant exposure. The underlying mechanism of prion propagation and the species barriers that control cross species transmission has been investigated quite extensively. So far a number of prion strains have been characterized and those have been intimately linked to species-specific infectivity and other pathophysiological manifestations. These strains are encoded by a protein-only agent, and have a high degree of sequence identity across mammalian species. The molecular events that lead to strain differentiation remain elusive. In order to contribute to the understanding of strain differentiation, we have determined the crystal structures of the globular, folded domains of four prion proteins (cow, deer, elk and Syrian hamster) bound to the POM1 antibody fragment Fab. Although the overall structural folds of the mammalian prion proteins remains extremely similar, there are several local structural v...Continue Reading

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Citations

Apr 28, 2017·Journal of Peptide Science : an Official Publication of the European Peptide Society·André Wuttke, Armin Geyer
Nov 14, 2017·PLoS Pathogens·Natalia Fernández-BorgesJoaquín Castilla
Sep 22, 2018·Journal of Computational Chemistry·Helen Nathalia ThompsonHubert Stassen

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