Prion protein self-peptides modulate prion interactions and conversion
نویسندگان
چکیده
منابع مشابه
Conformational conversion of prion protein in prion diseases.
Prion diseases are a group of infectious fatal neurodegenerative diseases. The conformational conversion of a cellular prion protein (PrP(C)) into an abnormal misfolded isoform (PrP(Sc)) is the key event in prion diseases pathology. Under normal conditions, the high-energy barrier separates PrP(C) from PrP(Sc) isoform. However, pathogenic mutations, modifications as well as some cofactors, such...
متن کاملSelf prion protein peptides are immunogenic in Lewis rats.
Prion diseases are caused by abnormal folding of the prion protein. The paradigm is that the prion protein is not immunogenic because the immune system must be tolerant to such a self protein. In an attempt to identify immunogenic prion peptides, we immunized Lewis rats with peptides that fitted the MHC class II RT1.B(1)motif. Both humoral and cellular immunity to the prion peptides were obtain...
متن کاملSonication induced intermediate in prion protein conversion.
We have observed that hamster prion protein (PrP(C)) undergoes conformational changes on exposure to heat or sonication. If a sonication induced new conformer is seeded with a small amount of its abnormal pathogenic isoform (PrP(Sc)) it undergoes a significant conversion to a proteinase-resistant isoform. This suggests the presence of a third stable PrP conformer, which may be intermediate in t...
متن کاملReview: prion protein and amyloid beta interactions
In 2009 it was discovered that prion protein (PrP) binds amyloid beta oligomers (Aβo), potentially acting as a receptor on the surface of neurons. PrP was additionally suggested to mediate at least some of the toxic effects of Aβo in Alzheimer’s disease (AD), a proposition which has proven enormously controversial. In the past three years, several studies have produced apparently strong evidenc...
متن کاملDestabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency
Prion diseases are infectious neurodegenerative disorders of humans and animals caused by misfolded forms of the cellular prion protein PrPC. Prions cause disease by converting PrPC into aggregation-prone PrPSc. Chronic wasting disease (CWD) is the most contagious prion disease with substantial lateral transmission, affecting free-ranging and farmed cervids. Although the PrP primary structure i...
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ژورنال
عنوان ژورنال: BMC Biochemistry
سال: 2009
ISSN: 1471-2091
DOI: 10.1186/1471-2091-10-29