Rapid cell-surface prion protein conversion revealed using a novel cell system
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چکیده
منابع مشابه
Rapid cell-surface prion protein conversion revealed using a novel cell system
Prion diseases are fatal neurodegenerative disorders with unique transmissible properties. The infectious and pathological agent is thought to be a misfolded conformer of the prion protein. Little is known about the initial events in prion infection because the infecting prion source has been immunologically indistinguishable from normal cellular prion protein (PrP(C)). Here we develop a unique...
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We used ELISA and flow cytometry to study the binding of prion protein PrP to glycosaminoglycans (GAGs). We found that recombinant human PrP (rPrP) binds GAGs including chondroitin sulphate A, chondroitin sulphate B, hyaluronic acid, and heparin. rPrP binding to GAGs occurs via the N-terminus, a region known to bind divalent cations. Additionally, rPrP binding to GAGs is enhanced in the presenc...
متن کاملCell biological studies of the prion protein.
Studying PrPC and PrPSc in cell culture systems is advantageous because such systems contain all the organelles, membranes, and molecular cofactors that are likely to play an important role in the biology of the proteins. Using cultured cells expressing PrPC, we have discovered that this isoform constitutively cycles between the cell surface and an endocytic compartment, a process that is media...
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In sheep polymorphisms of the prion gene (PRNP) at the codons 136, 154 and 171 strongly influence the susceptibility to scrapie and bovine spongiform encephalopathy (BSE) infections. In goats a number of other gene polymorphisms were found which are suspected to trigger similar effects. However, no strong correlation between polymorphisms and TSE susceptibility in goats has yet been obtained fr...
متن کاملGlycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification
Prions are formed of misfolded assemblies (PrP(Sc)) of the variably N-glycosylated cellular prion protein (PrP(C)). In infected species, prions replicate by seeding the conversion and polymerization of host PrP(C). Distinct prion strains can be recognized, exhibiting defined PrP(Sc) biochemical properties such as the glycotype and specific biological traits. While strain information is encoded ...
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ژورنال
عنوان ژورنال: Nature Communications
سال: 2011
ISSN: 2041-1723
DOI: 10.1038/ncomms1282