Abstract
Most of the diagnostic methods for transmissible spongiform encephalopathies are based on the detection of the abnormal protease-resistant conformers of the prion protein (PrPSc), when the normal protease-sensitive conformers (PrPC) are also present. A selective immune detection of PrPSc with high sensitivity is hampered by the absence of sufficient knowledge about the structure of PrPSc. An economical and rapid mapping approach is used here for the identification of epitopes that are exposed differently on PrPSc and PrPC. This approach revealed remarkable differences in the conformation/accessibility of the two long helical segments between the two prion forms. This result is not in harmony with recent models of PrPSc.
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.
