Non-infectious aggregates of the prion protein react with several PrPSc-directed antibodies
نویسندگان
چکیده
منابع مشابه
Amyloid aggregates of the HET-s prion protein are infectious.
The [Het-s] infectious element of the filamentous fungus Podospora anserina is a prion. We have recently reported that recombinant HET-s protein aggregates in vitro into amyloid fibers. In vivo, the protein aggregates specifically in the [Het-s] prion strains. Here, we show that biolistic introduction of aggregated recombinant HET-s protein into fungal cells induces emergence of the [Het-s] pri...
متن کاملPrPSc-Specific Antibodies with the Ability to Immunodetect Prion Oligomers
The development of antibodies with binding capacity towards soluble oligomeric forms of PrPSc recognised in the aggregation process in early stage of the disease would be of paramount importance in diagnosing prion diseases before extensive neuropathology has ensued. As blood transfusion appears to be efficient in the transmission of the infectious prion agent, there is an urgent need to develo...
متن کاملHeterogeneity of Abnormal Prion Protein (PrPSc) in Murine Scrapie Prions Determined by PrPSc-Specific Monoclonal Antibodies
In prion diseases, abnormal prion protein (PrP(Sc)) is considered as the main component of the infectious agent. Delineation of PrP(Sc) conformation is expected to be a critical factor in understanding properties of prions. However, practical methods to differentiate between conformers of PrP(Sc) are inadequate. Here, we used two PrP(Sc)-specific monoclonal antibodies (mAbs), 3B7 and 3H6, and f...
متن کاملMultiple biochemical similarities between infectious and non-infectious aggregates of a prion protein carrying an octapeptide insertion.
A nine-octapeptide insertion in the prion protein (PrP) gene is associated with an inherited form of human prion disease. Transgenic (Tg) mice that express the mouse homolog of this mutation (designated PG14) spontaneously accumulate in their brains an insoluble and weakly protease-resistant form of the mutant protein. This form (designated PG14(Spon)) is highly neurotoxic, but is not infectiou...
متن کاملPrPSc-like prion protein peptide inhibits the function of cellular prion protein.
Mice lacking expression of the prion protein are protected against infection with prion disease. Neurodegeneration in prion disease requires the formation of the abnormal isoform of the prion protein (PrP(Sc)) from host prion protein. Therefore expression of normal host prion protein is necessary for prion disease. In the present investigation, it was demonstrated that PrP(Sc) and a peptide res...
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ژورنال
عنوان ژورنال: Journal of Neurochemistry
سال: 2008
ISSN: 0022-3042
DOI: 10.1111/j.1471-4159.2008.05306.x