2017
DOI: 10.1371/journal.ppat.1006491
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Abstract: Prions, characterized by self-propagating protease-resistant prion protein (PrP) conformations, are agents causing prion disease. Recent studies generated several such self-propagating protease-resistant recombinant PrP (rPrP-res) conformers. While some cause prion disease, others fail to induce any pathology. Here we showed that although distinctly different, the pathogenic and non-pathogenic rPrP-res conformers were similarly recognized by a group of conformational antibodies against prions and shared a simi… Show more

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Cited by 32 publications
(45 citation statements)
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“…Initial characterization of rPrP-res RNA and rPrP-res RNA-low aggregates revealed that the PK-resistant core of rPrP-res RNA is approximately 1 kDa longer compared with that of rPrPres RNA-low (ϳ16 and 15 kDa, respectively) (27). However, using an arsenal of biochemical and immunochemical tools, we could not detect any other differences in the physicochemical properties of the two aggregate types (27).…”
mentioning
confidence: 63%
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“…Initial characterization of rPrP-res RNA and rPrP-res RNA-low aggregates revealed that the PK-resistant core of rPrP-res RNA is approximately 1 kDa longer compared with that of rPrPres RNA-low (ϳ16 and 15 kDa, respectively) (27). However, using an arsenal of biochemical and immunochemical tools, we could not detect any other differences in the physicochemical properties of the two aggregate types (27).…”
mentioning
confidence: 63%
“…Recently, it was shown that, in addition to these highly infectious rPrP-res RNA prions, using the same PMCA protocol and identical cofactors one can generate de novo another type of self-propagating rPrP-res aggregate, denoted rPrP-res RNA-low , that biochemically appears very similar to rPrP-res RNA but lacks any infectivity (26,27). The availability of these two selfpropagating aggregate types with dramatically different biological properties opened up new avenues for exploring the structural basis of prion infectivity.…”
mentioning
confidence: 99%
“…First structural studies on PrP C isolated from brains of SHas demonstrated a predominantly α‐helical content . As these measurements agreed well with subsequent spectroscopic data of recombinant PrP, accessible in larger amounts, it was considered an appropriate surrogate in biochemical experiments, as well as in solving nuclear magnetic resonance (NMR) and crystal structures of PrP . The PrP structure comprises an unstructured N ‐terminal (aa 23‐120) and a globular C ‐terminal part (aa 121‐231) (Figure ).…”
Section: Properties and Structures Of The Prpmentioning
confidence: 64%
“…Apart from the autocatalytic propagation of PrP Sc , another crucial hallmark of the PrP C ‐PrP Sc conversion is the de novo generation of infectivity. However, when inoculated into animals, PrP fibrillar assemblies can range from being biologically inert to fully infectious, pathogenic, and transmissible in subsequent passages . Legname and coworkers inoculated transgenic mice expressing truncated PrP C (aa 89‐231) with amyloid fibrils formed from recombinant PrP (aa 89‐230).…”
Section: Mechanism Of Prpc‐prpsc Conversionmentioning
confidence: 99%
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