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Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease.

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Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease. / Polymenidou, Magdalini; Stoeck, Katharina; Glatzel, Markus; Vey, Martin; Bellon, Anne; Aguzzi, Adriano.

In: LANCET NEUROL, Vol. 4, No. 12, 12, 2005, p. 805-814.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Polymenidou, M, Stoeck, K, Glatzel, M, Vey, M, Bellon, A & Aguzzi, A 2005, 'Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease.', LANCET NEUROL, vol. 4, no. 12, 12, pp. 805-814. <http://www.ncbi.nlm.nih.gov/pubmed/16297838?dopt=Citation>

APA

Polymenidou, M., Stoeck, K., Glatzel, M., Vey, M., Bellon, A., & Aguzzi, A. (2005). Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease. LANCET NEUROL, 4(12), 805-814. [12]. http://www.ncbi.nlm.nih.gov/pubmed/16297838?dopt=Citation

Vancouver

Polymenidou M, Stoeck K, Glatzel M, Vey M, Bellon A, Aguzzi A. Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease. LANCET NEUROL. 2005;4(12):805-814. 12.

Bibtex

@article{f18514608c3d4599ada576d27e401994,
title = "Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease.",
abstract = "BACKGROUND: The molecular typing of sporadic Creutzfeldt-Jakob disease (CJD) is based on the size and glycoform ratio of protease-resistant prion protein (PrP(Sc)), and on PRNP haplotype. On digestion with proteinase K, type 1 and type 2 PrP(Sc) display unglycosylated core fragments of 21 kDa and 19 kDa, resulting from cleavage around amino acids 82 and 97, respectively. METHODS: We generated anti-PrP monoclonal antibodies to epitopes immediately preceding the differential proteinase K cleavage sites. These antibodies, which were designated POM2 and POM12, recognise type 1, but not type 2, PrP(Sc). FINDINGS: We studied 114 brain samples from 70 patients with sporadic CJD and three patients with variant CJD. Every patient classified as CJD type 2, and all variant CJD patients, showed POM2/POM12 reactivity in the cerebellum and other PrP(Sc)-rich brain areas, with a typical PrP(Sc) type 1 migration pattern. INTERPRETATION: The regular coexistence of multiple PrP(Sc) types in patients with CJD casts doubts on the validity of electrophoretic PrP(Sc) mobilities as surrogates for prion strains, and questions the rational basis of current CJD classifications.",
author = "Magdalini Polymenidou and Katharina Stoeck and Markus Glatzel and Martin Vey and Anne Bellon and Adriano Aguzzi",
year = "2005",
language = "Deutsch",
volume = "4",
pages = "805--814",
journal = "LANCET NEUROL",
issn = "1474-4422",
publisher = "Lancet Publishing Group",
number = "12",

}

RIS

TY - JOUR

T1 - Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease.

AU - Polymenidou, Magdalini

AU - Stoeck, Katharina

AU - Glatzel, Markus

AU - Vey, Martin

AU - Bellon, Anne

AU - Aguzzi, Adriano

PY - 2005

Y1 - 2005

N2 - BACKGROUND: The molecular typing of sporadic Creutzfeldt-Jakob disease (CJD) is based on the size and glycoform ratio of protease-resistant prion protein (PrP(Sc)), and on PRNP haplotype. On digestion with proteinase K, type 1 and type 2 PrP(Sc) display unglycosylated core fragments of 21 kDa and 19 kDa, resulting from cleavage around amino acids 82 and 97, respectively. METHODS: We generated anti-PrP monoclonal antibodies to epitopes immediately preceding the differential proteinase K cleavage sites. These antibodies, which were designated POM2 and POM12, recognise type 1, but not type 2, PrP(Sc). FINDINGS: We studied 114 brain samples from 70 patients with sporadic CJD and three patients with variant CJD. Every patient classified as CJD type 2, and all variant CJD patients, showed POM2/POM12 reactivity in the cerebellum and other PrP(Sc)-rich brain areas, with a typical PrP(Sc) type 1 migration pattern. INTERPRETATION: The regular coexistence of multiple PrP(Sc) types in patients with CJD casts doubts on the validity of electrophoretic PrP(Sc) mobilities as surrogates for prion strains, and questions the rational basis of current CJD classifications.

AB - BACKGROUND: The molecular typing of sporadic Creutzfeldt-Jakob disease (CJD) is based on the size and glycoform ratio of protease-resistant prion protein (PrP(Sc)), and on PRNP haplotype. On digestion with proteinase K, type 1 and type 2 PrP(Sc) display unglycosylated core fragments of 21 kDa and 19 kDa, resulting from cleavage around amino acids 82 and 97, respectively. METHODS: We generated anti-PrP monoclonal antibodies to epitopes immediately preceding the differential proteinase K cleavage sites. These antibodies, which were designated POM2 and POM12, recognise type 1, but not type 2, PrP(Sc). FINDINGS: We studied 114 brain samples from 70 patients with sporadic CJD and three patients with variant CJD. Every patient classified as CJD type 2, and all variant CJD patients, showed POM2/POM12 reactivity in the cerebellum and other PrP(Sc)-rich brain areas, with a typical PrP(Sc) type 1 migration pattern. INTERPRETATION: The regular coexistence of multiple PrP(Sc) types in patients with CJD casts doubts on the validity of electrophoretic PrP(Sc) mobilities as surrogates for prion strains, and questions the rational basis of current CJD classifications.

M3 - SCORING: Zeitschriftenaufsatz

VL - 4

SP - 805

EP - 814

JO - LANCET NEUROL

JF - LANCET NEUROL

SN - 1474-4422

IS - 12

M1 - 12

ER -