ArticleBMC biochemistry2009
Prion protein self-peptides modulate prion interactions and conversion.
Article in BMC biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- The manifold role of octapeptide repeats in prion protein assembly.Peptide science (Hoboken, N.J.) · 2023Article
- Oxidative and Inflammatory Events in Prion Diseases: Can They Be Therapeutic Targets?Current aging science · 2019Review
- Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular Dynamics.Journal of chemical theory and computation · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMolecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrP(C)) into the scrapie associated isoform (PrP(Sc)), are poorly understood. Selective self-interaction between PrP molecules forms a basis underlying the observed differences of the PrP(C) into PrP(Sc) conversion process (agent replication). The importance of previously peptide-scanning mapped ovine PrP self-interaction domains on this conversion was investigated by studying the ability of six of these ovine PrP based peptides to modulate two processes; PrP self-interaction and conversion.
resultsThree peptides (octarepeat, binding domain 2 -and C-terminal) were capable of inhibiting self-interaction of PrP in a solid-phase PrP peptide array. Three peptides (N-terminal, binding domain 2, and amyloidogenic motif) modulated prion conversion when added before or after initiation of the prion protein misfolding cyclic amplification (PMCA) reaction using brain homogenates. The C-terminal peptides (core region and C-terminal) only affected conversion (increased PrP(res) formation) when added before mixing PrP(C) and PrP(Sc), whereas the octarepeat peptide only affected conversion when added after this mixing.
conclusionThis study identified the putative PrP core binding domain that facilitates the PrP(C)-PrP(Sc) interaction (not conversion), corroborating evidence that the region of PrP containing this domain is important in the species-barrier and/or scrapie susceptibility. The octarepeats can be involved in PrP(C)-PrP(Sc) stabilization, whereas the N-terminal glycosaminoglycan binding motif and the amyloidogenic motif indirectly affected conversion. Binding domain 2 and the C-terminal domain are directly implicated in PrP(C) self-interaction during the conversion process and may prove to be prime targets in new therapeutic strategy development, potentially retaining PrP(C) function. These results emphasize the importance of probable PrP(C)-PrP(C) and required PrP(C)-PrP(Sc) interactions during PrP conversion. All interactions are probably part of the complex process in which polymorphisms and species barriers affect TSE transmission and susceptibility.
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