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Preclinical deposition of pathological prion protein in muscle of experimentally infected primates.

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Preclinical deposition of pathological prion protein in muscle of experimentally infected primates. / Krasemann, Susanne; Neumann, Melanie; Geissen, Markus; Bodemer, Walter; Kaup, Franz-Josef; Schulz-Schaeffer, Walter; Morel, Nathalie; Aguzzi, Adriano; Glatzel, Markus.

In: PLOS ONE, Vol. 5, No. 11, 11, 2010, p. 13906.

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

Harvard

Krasemann, S, Neumann, M, Geissen, M, Bodemer, W, Kaup, F-J, Schulz-Schaeffer, W, Morel, N, Aguzzi, A & Glatzel, M 2010, 'Preclinical deposition of pathological prion protein in muscle of experimentally infected primates.', PLOS ONE, vol. 5, no. 11, 11, pp. 13906. https://doi.org/10.1371/journal.pone.0013906

APA

Krasemann, S., Neumann, M., Geissen, M., Bodemer, W., Kaup, F-J., Schulz-Schaeffer, W., Morel, N., Aguzzi, A., & Glatzel, M. (2010). Preclinical deposition of pathological prion protein in muscle of experimentally infected primates. PLOS ONE, 5(11), 13906. [11]. https://doi.org/10.1371/journal.pone.0013906

Vancouver

Krasemann S, Neumann M, Geissen M, Bodemer W, Kaup F-J, Schulz-Schaeffer W et al. Preclinical deposition of pathological prion protein in muscle of experimentally infected primates. PLOS ONE. 2010;5(11):13906. 11. https://doi.org/10.1371/journal.pone.0013906

Bibtex

@article{0cc116d16b86418aa62fe9058925969e,
title = "Preclinical deposition of pathological prion protein in muscle of experimentally infected primates.",
abstract = "Prion diseases are transmissible fatal neurodegenerative disorders affecting humans and animals. A central step in disease progression is the accumulation of a misfolded form (PrP(Sc)) of the host encoded prion protein (PrP(C)) in neuronal and non-neuronal tissues. The involvement of peripheral tissues in preclinical states increases the risk of accidental transmission. On the other hand, detection of PrP(Sc) in non-neuronal easy-accessible compartments such as muscle may offer a novel diagnostic tool. Primate models have proven invaluable to investigate prion diseases. We have studied the deposition of PrP(Sc) in muscle and central nervous system of rhesus monkeys challenged with sporadic Creutzfeldt-Jakob disease (sCJD), variant CJD (vCJD) and bovine spongiform encephalopathy (BSE) in preclinical and clinical stage using biochemical and morphological methods. Here, we show the preclinical presence of PrP(Sc) in muscle and central nervous system of rhesus monkeys experimentally infected with vCJD.",
author = "Susanne Krasemann and Melanie Neumann and Markus Geissen and Walter Bodemer and Franz-Josef Kaup and Walter Schulz-Schaeffer and Nathalie Morel and Adriano Aguzzi and Markus Glatzel",
year = "2010",
doi = "10.1371/journal.pone.0013906",
language = "Deutsch",
volume = "5",
pages = "13906",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "11",

}

RIS

TY - JOUR

T1 - Preclinical deposition of pathological prion protein in muscle of experimentally infected primates.

AU - Krasemann, Susanne

AU - Neumann, Melanie

AU - Geissen, Markus

AU - Bodemer, Walter

AU - Kaup, Franz-Josef

AU - Schulz-Schaeffer, Walter

AU - Morel, Nathalie

AU - Aguzzi, Adriano

AU - Glatzel, Markus

PY - 2010

Y1 - 2010

N2 - Prion diseases are transmissible fatal neurodegenerative disorders affecting humans and animals. A central step in disease progression is the accumulation of a misfolded form (PrP(Sc)) of the host encoded prion protein (PrP(C)) in neuronal and non-neuronal tissues. The involvement of peripheral tissues in preclinical states increases the risk of accidental transmission. On the other hand, detection of PrP(Sc) in non-neuronal easy-accessible compartments such as muscle may offer a novel diagnostic tool. Primate models have proven invaluable to investigate prion diseases. We have studied the deposition of PrP(Sc) in muscle and central nervous system of rhesus monkeys challenged with sporadic Creutzfeldt-Jakob disease (sCJD), variant CJD (vCJD) and bovine spongiform encephalopathy (BSE) in preclinical and clinical stage using biochemical and morphological methods. Here, we show the preclinical presence of PrP(Sc) in muscle and central nervous system of rhesus monkeys experimentally infected with vCJD.

AB - Prion diseases are transmissible fatal neurodegenerative disorders affecting humans and animals. A central step in disease progression is the accumulation of a misfolded form (PrP(Sc)) of the host encoded prion protein (PrP(C)) in neuronal and non-neuronal tissues. The involvement of peripheral tissues in preclinical states increases the risk of accidental transmission. On the other hand, detection of PrP(Sc) in non-neuronal easy-accessible compartments such as muscle may offer a novel diagnostic tool. Primate models have proven invaluable to investigate prion diseases. We have studied the deposition of PrP(Sc) in muscle and central nervous system of rhesus monkeys challenged with sporadic Creutzfeldt-Jakob disease (sCJD), variant CJD (vCJD) and bovine spongiform encephalopathy (BSE) in preclinical and clinical stage using biochemical and morphological methods. Here, we show the preclinical presence of PrP(Sc) in muscle and central nervous system of rhesus monkeys experimentally infected with vCJD.

U2 - 10.1371/journal.pone.0013906

DO - 10.1371/journal.pone.0013906

M3 - SCORING: Zeitschriftenaufsatz

VL - 5

SP - 13906

JO - PLOS ONE

JF - PLOS ONE

SN - 1932-6203

IS - 11

M1 - 11

ER -