Genotype frequencies at codon 129 of the Prion Protein Gene in Brazil: implications in susceptibility to variant Creutzfeldt--Jakob disease compared to European and Asian populations

2005 ◽  
Vol 20 (7) ◽  
pp. 593-595 ◽  
Author(s):  
Erich Vinicius de Paula ◽  
Marcelo Addas-Carvalho ◽  
Devanira Souza Paixao Costa ◽  
Sara Terezinha Olalla Saad ◽  
Simone Cristina Olenscki Gilli
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Prion Protein Gene ◽  
Asian Populations ◽  
Genotype Frequencies ◽  
Jakob Disease ◽  
Codon 129

scholarly journals Codon 129 polymorphism of prion protein gene in is not a risk factor for Alzheimer's disease

2013 ◽  
Vol 71 (7) ◽  
pp. 423-427 ◽  
Author(s):  
Jerusa Smid ◽  
Michele Christine Landemberger ◽  
Valéria Santoro Bahia ◽  
Vilma Regina Martins ◽  
Ricardo Nitrini
Keyword(s):  
Risk Factor ◽  
Cognitive Performance ◽  
Prion Protein ◽  
Protein Gene ◽  
Apoe Genotype ◽  
Genotype Distribution ◽  
Prion Protein Gene ◽  
Apolipoprotein E Gene ◽  
Jakob Disease ◽  
Codon 129

Interaction of prion protein and amyloid-b oligomers has been demonstrated recently. Homozygosity at prion protein gene (PRNP) codon 129 is associated with higher risk for Creutzfeldt-Jakob disease. This polymorphism has been addressed as a possible risk factor in Alzheimer disease (AD).ObjectiveTo describe the association between codon 129 polymorphisms and AD.MethodsWe investigated the association of codon 129 polymorphism of PRNP in 99 AD patients and 111 controls, and the association between this polymorphism and cognitive performance. Other polymorphisms of PRNP and additive effect of apolipoprotein E gene (ApoE) were evaluated.ResultsCodon 129 genotype distribution in AD 45.5% methionine (MM), 42.2% methionine valine (MV), 12.1% valine (VV); and 39.6% MM, 50.5% MV, 9.9% VV among controls (p>0.05). There were no differences of cognitive performance concerning codon 129. Stratification according to ApoE genotype did not reveal difference between groups.ConclusionCodon 129 polymorphism is not a risk factor for AD in Brazilian patients.

A novel phenotype in familial Creutzfeldt-Jakob disease: Prion protein gene E200K mutation coupled with valine at codon 129 and type 2 protease-resistant prion protein

1999 ◽  
Vol 45 (6) ◽  
pp. 812-816 ◽  
Author(s):  
Johannes A. Hainfellner ◽  
Piero Parchi ◽  
Tetsuyuki Kitamoto ◽  
Christa Jarius ◽  
Pierluigi Gambetti ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Prion Protein Gene ◽  
E200k Mutation ◽  
Jakob Disease ◽  
Codon 129

scholarly journals Prion Strain Characterization of a Novel Subtype of Creutzfeldt-Jakob Disease

2017 ◽  
Vol 91 (11) ◽  
Author(s):  
Roberta Galeno ◽  
Michele Angelo Di Bari ◽  
Romolo Nonno ◽  
Franco Cardone ◽  
Marco Sbriccoli ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Prion Protein ◽  
Protein Gene ◽  
Prion Protein Gene ◽  
Prion Strain ◽  
Bank Voles ◽  
Jakob Disease ◽  
Codon 129

ABSTRACT In 2007, we reported a patient with an atypical form of Creutzfeldt-Jakob disease (CJD) heterozygous for methionine-valine (MV) at codon 129 who showed a novel pathological prion protein (PrPTSE) conformation with an atypical glycoform (AG) profile and intraneuronal PrP deposition. In the present study, we further characterize the conformational properties of this pathological prion protein (PrPTSE MVAG), showing that PrPTSE MVAG is composed of multiple conformers with biochemical properties distinct from those of PrPTSE type 1 and type 2 of MV sporadic CJD (sCJD). Experimental transmission of CJD-MVAG to bank voles and gene-targeted transgenic mice carrying the human prion protein gene (TgHu mice) showed unique transmission rates, survival times, neuropathological changes, PrPTSE deposition patterns, and PrPTSE glycotypes that are distinct from those of sCJD-MV1 and sCJD-MV2. These biochemical and experimental data suggest the presence of a novel prion strain in CJD-MVAG. IMPORTANCE Sporadic Creutzfeldt-Jakob disease is caused by the misfolding of the cellular prion protein, which assumes two different major conformations (type 1 and type 2) and, together with the methionine/valine polymorphic codon 129 of the prion protein gene, contribute to the occurrence of distinct clinical-pathological phenotypes. Inoculation in laboratory rodents of brain tissues from the six possible combinations of pathological prion protein types with codon 129 genotypes results in the identification of 3 or 4 strains of prions. We report on the identification of a novel strain of Creutzfeldt-Jakob disease isolated from a patient who carried an abnormally glycosylated pathological prion protein. This novel strain has unique biochemical characteristics, does not transmit to humanized transgenic mice, and shows exclusive transmission properties in bank voles. The identification of a novel human prion strain improves our understanding of the pathogenesis of the disease and of possible mechanisms of prion transmission.

Prion protein gene analysis in new variant cases of Creutzfeldt-Jakob disease

The Lancet ◽  
1996 ◽  
Vol 348 (9019) ◽  
pp. 56 ◽  
Author(s):  
John Collinge ◽  
Jonathan Beck ◽  
Tracy Campbell ◽  
Kathy Estibeiro ◽  
Robert G Will
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Gene Analysis ◽  
Prion Protein Gene ◽  
New Variant ◽  
Jakob Disease

Novel prion protein gene mutation at codon 196 (E196A) in a septuagenarian with Creutzfeldt–Jakob disease

2014 ◽  
Vol 21 (1) ◽  
pp. 175-178 ◽  
Author(s):  
Hongliang Zhang ◽  
Meibo Wang ◽  
Limin Wu ◽  
Haining Zhang ◽  
Tao Jin ◽  
...  
Keyword(s):  
Prion Protein ◽  
Gene Mutation ◽  
Protein Gene ◽  
Prion Protein Gene ◽  
Jakob Disease

scholarly journals The First Meta-Analysis of the M129V Single-Nucleotide Polymorphism (SNP) of the Prion Protein Gene (PRNP) with Sporadic Creutzfeldt–Jakob Disease

Cells ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 3132
Author(s):  
Yong-Chan Kim ◽  
Byung-Hoon Jeong
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Meta Analysis ◽  
Prnp Gene ◽  
Case Control ◽  
Prion Protein Gene ◽  
Nucleotide Polymorphism ◽  
Single Nucleotide ◽  
Jakob Disease ◽  
Sporadic Cjd

Prion diseases are fatal, chronic, and incurable neurodegenerative diseases caused by pathogenic forms of prion protein (PrPSc) derived from endogenous forms of prion protein (PrPC). Several case–control and genome-wide association studies have reported that the M129V polymorphism of the human prion protein gene (PRNP) is significantly associated with susceptibility to sporadic Creutzfeldt–Jakob disease (CJD). However, since some case–control studies have not shown these associations, the results remain controversial. We collected data that contain the genotype and allele frequencies of the M129V single-nucleotide polymorphism (SNP) of the PRNP gene and information on ethnic backgrounds from sporadic CJD patients. We performed a meta-analysis by collecting data from eligible studies to evaluate the association between the M129V SNP of the PRNP gene and susceptibility to sporadic CJD. We found a very strong association between the M129V SNP of the PRNP gene and susceptibility to sporadic CJD using a meta-analysis for the first time. We validated the eligibility of existing reports and found severe heterogeneity in some previous studies. We also found that the MM homozygote is a potent risk factor for sporadic CJD compared to the MV heterozygote in the heterozygote comparison model (MM vs. MV, odds ratio = 4.9611, 95% confidence interval: 3.4785; 7.0758, p < 1 × 10−10). To the best of our knowledge, this was the first meta-analysis assessment of the relationship between the M129V SNP of the PRNP gene and susceptibility to sporadic CJD.

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