ArticleThe Journal of biological chemistry2012
Characterization of conformation-dependent prion protein epitopes.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 30 citations in OpenAlex.
- Distinct prion conformers from brain and peripheral tissues of gene-targeted mice produce convergent CWD strain properties.PLoS pathogens · 2026Article
- Regulated coexpression of PrP from different species in mice impacts the replication and host range properties of prion strains.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Strain Properties of Korean and North American Chronic Wasting Disease Prions Are Indistinguishable.The Journal of infectious diseases · 2025Article
- Article
- Novel Prion Strain as Cause of Chronic Wasting Disease in a Moose, Finland.Emerging infectious diseases · 2023Article
- Structure of prion β-oligomers as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations.Proteomics · 2021Article
- Article
- Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination.The Journal of biological chemistry · 2020Article
- Direct interaction of DNMT inhibitors to PrPActa pharmaceutica Sinica. B · 2019Article
- Primary structural differences at residue 226 of deer and elk PrP dictate selection of distinct CWD prion strains in gene-targeted mice.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- An Amino Acid Substitution Found in Animals with Low Susceptibility to Prion Diseases Confers a Protective Dominant-Negative Effect in Prion-Infected Transgenic Mice.Molecular neurobiology · 2018Article
- Effect of poly-L-arginine in inhibiting scrapie prion protein of cultured cells.Molecular and cellular biochemistry · 2017Article
- Prion replication without host adaptation during interspecies transmissions.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- PrPC expression and prion seeding activity in the alimentary tract and lymphoid tissue of deer.PloS one · 2017Article
- Prion Diagnosis: Application of Real-Time Quaking-Induced Conversion.BioMed research international · 2017Review
- Insights into Mechanisms of Transmission and Pathogenesis from Transgenic Mouse Models of Prion Diseases.Methods in molecular biology (Clifton, N.J.) · 2017Review
- Detection of misfolded protein aggregates from a clinical perspective.Journal of clinical and translational research · 2016Review
- A transfectant RK13 cell line permissive to classical caprine scrapie prion propagation.Prion · 2016Article
- Conformation-dependent epitopes recognized by prion protein antibodies probed using mutational scanning and deep sequencing.Journal of molecular biology · 2015Article
- Characterization of four new monoclonal antibodies against the distal N-terminal region of PrP(c).PeerJ · 2015Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
Abstract
Whereas prion replication involves structural rearrangement of cellular prion protein (PrP(C)), the existence of conformational epitopes remains speculative and controversial, and PrP transformation is monitored by immunoblot detection of PrP(27-30), a protease-resistant counterpart of the pathogenic scrapie form (PrP(Sc)) of PrP. We now describe the involvement of specific amino acids in conformational determinants of novel monoclonal antibodies (mAbs) raised against randomly chimeric PrP. Epitope recognition of two mAbs depended on polymorphisms controlling disease susceptibility. Detection by one, referred to as PRC5, required alanine and asparagine at discontinuous mouse PrP residues 132 and 158, which acquire proximity when residues 126-218 form a structured globular domain. The discontinuous epitope of glycosylation-dependent mAb PRC7 also mapped within this domain at residues 154 and 185. In accordance with their conformational dependence, tertiary structure perturbations compromised recognition by PRC5, PRC7, as well as previously characterized mAbs whose epitopes also reside in the globular domain, whereas conformation-independent epitopes proximal or distal to this region were refractory to such destabilizing treatments. Our studies also address the paradox of how conformational epitopes remain functional following denaturing treatments and indicate that cellular PrP and PrP(27-30) both renature to a common structure that reconstitutes the globular domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.