Abstract
Publisher Summary PrP associated with TSE disease (PrP-res) can induce its own formation, an essential prerequisite for a protein-only infectious agent. This “replication” is clearly influenced by prion protein (PrP) primary sequence and conformation. Supporting data are now available for how, in the absence of any nucleic acid component, these variations in PrP sequence and conformation could account for TSE species and strain characteristics. As a transmissible neurodegenerative disease, involving protein misfolding and amyloid formation, the TSE diseases are undoubtedly biologically unique. The question remains whether PrP-res alone can directly dictate all aspects of TSE pathogenesis or whether as yet unidentified factors or more conventional viral components are also involved.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
