ArticleEmerging infectious diseases2014
Variably protease-sensitive prionopathy, a unique prion variant with inefficient transmission properties.
Article in Emerging infectious diseases, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Search for a genetic cause of variably protease-sensitive prionopathy.PLoS pathogens · 2025Article
- Characterization of variably protease-sensitive prionopathy by capillary electrophoresis.Scientific reports · 2024Article
- Transmission of cervid prions to humanized mice demonstrates the zoonotic potential of CWD.Acta neuropathologica · 2022Article
- Phenotypic Heterogeneity of Variably Protease-Sensitive Prionopathy: A Report of Three Cases Carrying Different Genotypes atViruses · 2022Article
- Further Characterization of Glycoform-Selective Prions of Variably Protease-Sensitive Prionopathy.Pathogens (Basel, Switzerland) · 2021Article
- Challenges and Advances in Antemortem Diagnosis of Human Transmissible Spongiform Encephalopathies.Frontiers in bioengineering and biotechnology · 2020Review
- In Vitro Seeding Activity of Glycoform-Deficient Prions from Variably Protease-Sensitive Prionopathy and Familial CJD Associated with PrPMolecular neurobiology · 2019Article
- Variably protease-sensitive prionopathy: A differential diagnostic consideration for dementia.Neurology. Clinical practice · 2019Review
- Understanding Prion Strains: Evidence from Studies of the Disease Forms Affecting Humans.Viruses · 2019Review
- Variable Protease-Sensitive Prionopathy Transmission to Bank Voles.Emerging infectious diseases · 2019Article
- Prion disease: experimental models and reality.Acta neuropathologica · 2017Review
- Sporadic and Infectious Human Prion Diseases.Cold Spring Harbor perspectives in medicine · 2017Review
- Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2.PloS one · 2017Article
- Insights into Mechanisms of Transmission and Pathogenesis from Transgenic Mouse Models of Prion Diseases.Methods in molecular biology (Clifton, N.J.) · 2017Review
- Evaluating the Species Barrier.Food safety (Tokyo, Japan) · 2016Review
- Prions: Beyond a Single Protein.Clinical microbiology reviews · 2016Review
- Insights into Mechanisms of Chronic Neurodegeneration.International journal of molecular sciences · 2016Review
- The elusive role of the prion protein and the mechanism of toxicity in prion disease.PLoS pathogens · 2015Review
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13 authors.
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Abstract
Variably protease-sensitive prionopathy (VPSPr) can occur in persons of all codon 129 genotypes in the human prion protein gene (PRNP) and is characterized by a unique biochemical profile when compared with other human prion diseases. We investigated transmission properties of VPSPr by inoculating transgenic mice expressing human PRNP with brain tissue from 2 persons with the valine-homozygous (VV) and 1 with the heterozygous methionine/valine codon 129 genotype. No clinical signs or vacuolar pathology were observed in any inoculated mice. Small deposits of prion protein accumulated in the brains of inoculated mice after challenge with brain material from VV VPSPr patients. Some of these deposits resembled microplaques that occur in the brains of VPSPr patients. Comparison of these transmission properties with those of sporadic Creutzfeldt-Jakob disease in the same lines of mice indicated that VPSPr has distinct biological properties. Moreover, we established that VPSPr has limited potential for human-to-human transmission.
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