scholarly journals Phenotypic heterogeneity in inherited prion disease (P102L) is associated with differential propagation of protease-resistant wild-type and mutant prion protein

Brain ◽  
2006 ◽  
Vol 129 (6) ◽  
pp. 1557-1569 ◽  
Author(s):  
J. D. F. Wadsworth
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Phenotypic Heterogeneity ◽  
Wild Type

Insoluble wild–type and protease–resistant mutant prion protein in brains of patients with inherited prion disease

1996 ◽  
Vol 2 (1) ◽  
pp. 59-64 ◽  
Author(s):  
Ruth Gabizon ◽  
Glenn Telling ◽  
Zeev Meiner ◽  
Michele Halimi ◽  
Irit Kahana ◽  
...  
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Resistant Mutant ◽  
Wild Type

scholarly journals Recombinant prion protein induces a new transmissible prion disease in wild-type animals

2010 ◽  
Vol 119 (2) ◽  
pp. 177-187 ◽  
Author(s):  
Natallia Makarava ◽  
Gabor G. Kovacs ◽  
Olga Bocharova ◽  
Regina Savtchenko ◽  
Irina Alexeeva ◽  
...  
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Wild Type ◽  
Recombinant Prion Protein

scholarly journals The First Report of the Prion Protein Gene (PRNP) Sequence in Pekin Ducks (Anas platyrhynchos domestica): The Potential Prion Disease Susceptibility in Ducks

Genes ◽  
2021 ◽  
Vol 12 (2) ◽  
pp. 193
Author(s):  
Min-Ju Jeong ◽  
Yong-Chan Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Prion Protein ◽  
Dna Sequence ◽  
Prion Disease ◽  
Protein Gene ◽  
Prnp Gene ◽  
Pekin Duck ◽  
Prion Protein Gene ◽  
First Report ◽  
Aggregation Propensity ◽  
Pekin Ducks

Pathogenic prion protein (PrPSc), converted from normal prion protein (PrPC), causes prion disease. Although prion disease has been reported in several mammalian species, chickens are known to show strong resistance to prion diseases. In addition to chickens, the domestic duck occupies a large proportion in the poultry industry and may be regarded as a potential resistant host against prion disease. However, the DNA sequence of the prion protein gene (PRNP) has not been reported in domestic ducks. Here, we performed amplicon sequencing targeting the duck PRNP gene with the genomic DNA of Pekin ducks. In addition, we aligned the PrP sequence of the Pekin duck with that of various species using ClustalW2 and carried out phylogenetic analysis using Molecular Evolutionary Genetics Analysis X (MEGA X). We also constructed the structural modeling of the tertiary and secondary structures in avian PrP using SWISS-MODEL. Last, we investigated the aggregation propensity on Pekin duck PrP using AMYCO. We first reported the DNA sequence of the PRNP gene in Pekin ducks and found that the PrP sequence of Pekin ducks is more similar to that of geese than to that of chickens and mallards (wild ducks). Interestingly, Pekin duck PrP showed a high proportion of β-sheets compared to that of chicken PrP, and a high aggregation propensity compared to that of avian PrPs. However, Pekin duck PrP with substitutions of chicken-specific amino acids showed reduced aggregation propensities. To the best of our knowledge, this is the first report on the genetic characteristics of the PRNP sequence in Pekin ducks.

Detection of cutaneous prion protein deposits could help diagnose GPI‐anchorless prion disease with neuropathy

2021 ◽  
Author(s):  
Hiroyuki Honda ◽  
Kosuke Matsuzono ◽  
Kota Satoh ◽  
Masayoshi Fujisawa ◽  
Satoshi O. Suzuki ◽  
...  
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Protein Deposits

scholarly journals Doxycycline control of prion protein transgene expression modulates prion disease in mice

1998 ◽  
Vol 95 (21) ◽  
pp. 12580-12585 ◽  
Author(s):  
P. Tremblay ◽  
Z. Meiner ◽  
M. Galou ◽  
C. Heinrich ◽  
C. Petromilli ◽  
...  
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Transgene Expression

scholarly journals Genetic human prion disease modelled in PrP transgenic Drosophila

2017 ◽  
Vol 474 (19) ◽  
pp. 3253-3267 ◽  
Author(s):  
Alana M. Thackray ◽  
Alzbeta Cardova ◽  
Hanna Wolf ◽  
Lydia Pradl ◽  
Ina Vorberg ◽  
...  
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Prion Diseases ◽  
Principal Component ◽  
Site Directed Mutagenesis ◽  
Host Protein ◽  
Therapeutic Interventions ◽  
Proteinase K ◽  
Human Prion Disease ◽  
Transgenic Drosophila

Inherited human prion diseases, such as fatal familial insomnia (FFI) and familial Creutzfeldt–Jakob disease (fCJD), are associated with autosomal dominant mutations in the human prion protein gene PRNP and accumulation of PrPSc, an abnormal isomer of the normal host protein PrPC, in the brain of affected individuals. PrPSc is the principal component of the transmissible neurotoxic prion agent. It is important to identify molecular pathways and cellular processes that regulate prion formation and prion-induced neurotoxicity. This will allow identification of possible therapeutic interventions for individuals with, or at risk from, genetic human prion disease. Increasingly, Drosophila has been used to model human neurodegenerative disease. An important unanswered question is whether genetic prion disease with concomitant spontaneous prion formation can be modelled in Drosophila. We have used pUAST/PhiC31-mediated site-directed mutagenesis to generate Drosophila transgenic for murine or hamster PrP (prion protein) that carry single-codon mutations associated with genetic human prion disease. Mouse or hamster PrP harbouring an FFI (D178N) or fCJD (E200K) mutation showed mild Proteinase K resistance when expressed in Drosophila. Adult Drosophila transgenic for FFI or fCJD variants of mouse or hamster PrP displayed a spontaneous decline in locomotor ability that increased in severity as the flies aged. Significantly, this mutant PrP-mediated neurotoxic fly phenotype was transferable to recipient Drosophila that expressed the wild-type form of the transgene. Collectively, our novel data are indicative of the spontaneous formation of a PrP-dependent neurotoxic phenotype in FFI- or CJD-PrP transgenic Drosophila and show that inherited human prion disease can be modelled in this invertebrate host.

scholarly journals Expression of the Prion Protein Family Member Shadoo Causes Drug Hypersensitivity That Is Diminished by the Coexpression of the Wild Type Prion Protein

2015 ◽  
Vol 291 (9) ◽  
pp. 4473-4486 ◽  
Author(s):  
Antal Nyeste ◽  
Petra Bencsura ◽  
István Vida ◽  
Zoltán Hegyi ◽  
László Homolya ◽  
...  
Keyword(s):  
Family Member ◽  
Prion Protein ◽  
Drug Hypersensitivity ◽  
Protein Family ◽  
Wild Type
Sign in / Sign up

Export Citation Format

Share Document