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Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity.

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Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity. / Krasemann, Susanne; Neumann, Melanie; Szalay, Beata; Stocking, Carol; Glatzel, Markus.

In: J GEN VIROL, Vol. 94, No. Pt 2, Pt 2, 2013, p. 453-463.

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

Harvard

Krasemann, S, Neumann, M, Szalay, B, Stocking, C & Glatzel, M 2013, 'Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity.', J GEN VIROL, vol. 94, no. Pt 2, Pt 2, pp. 453-463. https://doi.org/10.1099/vir.0.045922-0

APA

Krasemann, S., Neumann, M., Szalay, B., Stocking, C., & Glatzel, M. (2013). Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity. J GEN VIROL, 94(Pt 2), 453-463. [Pt 2]. https://doi.org/10.1099/vir.0.045922-0

Vancouver

Krasemann S, Neumann M, Szalay B, Stocking C, Glatzel M. Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity. J GEN VIROL. 2013;94(Pt 2):453-463. Pt 2. https://doi.org/10.1099/vir.0.045922-0

Bibtex

@article{0dc7a66c440241f79ac5798ada83aef4,
title = "Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity.",
abstract = "Prion diseases are fatal neurodegenerative disorders. An important step in disease pathophysiology is the conversion of cellular prion protein (PrP(C)) to disease-associated misfolded conformers (PrP(Sc)). These misfolded PrP variants are a common component of prion infectivity and are detectable in diseased brain and lymphoreticular organs such as spleen. In the latter, PrP(Sc) is thought to replicate mainly in follicular dendritic cells within spleen follicles. Although the presence of PrP(Sc) is a hallmark for prion disease and serves as a main diagnostic criterion, in certain instances the amount of PrP(Sc) does not correlate well with neurotoxicity or prion infectivity. Therefore, it has been proposed that prions might be a mixture of different conformers and aggregates with differing properties. This study investigated the impact of disruption of spleen architecture by neoplasia on the abundance of different PrP species in spleens of prion-infected mice. Although follicular integrity was completely disturbed, titres of prion infectivity in neoplastic spleens were not significantly altered, yet no protease-resistant PrP(Sc) was detectable. Instead, unique protease-sensitive prion species could be detected in neoplastic spleens. These results indicate the dissociation of PrP(Sc) and prion infectivity and showed the presence of non-PrP(Sc) PrP species in spleen with divergent biochemical properties that become apparent after tissue architecture disruption.",
keywords = "Animals, Disease Models, Animal, Mice, Spleen/*pathology, Peptide Hydrolases/*metabolism, Prion Diseases/*complications/pathology, Prions/classification/*isolation & purification/*metabolism, Splenic Neoplasms/*complications/pathology, Animals, Disease Models, Animal, Mice, Spleen/*pathology, Peptide Hydrolases/*metabolism, Prion Diseases/*complications/pathology, Prions/classification/*isolation & purification/*metabolism, Splenic Neoplasms/*complications/pathology",
author = "Susanne Krasemann and Melanie Neumann and Beata Szalay and Carol Stocking and Markus Glatzel",
year = "2013",
doi = "10.1099/vir.0.045922-0",
language = "English",
volume = "94",
pages = "453--463",
journal = "J GEN VIROL",
issn = "0022-1317",
publisher = "Society for General Microbiology",
number = "Pt 2",

}

RIS

TY - JOUR

T1 - Protease-sensitive prion species in neoplastic spleens of prion-infected mice with uncoupling of PrP(Sc) and prion infectivity.

AU - Krasemann, Susanne

AU - Neumann, Melanie

AU - Szalay, Beata

AU - Stocking, Carol

AU - Glatzel, Markus

PY - 2013

Y1 - 2013

N2 - Prion diseases are fatal neurodegenerative disorders. An important step in disease pathophysiology is the conversion of cellular prion protein (PrP(C)) to disease-associated misfolded conformers (PrP(Sc)). These misfolded PrP variants are a common component of prion infectivity and are detectable in diseased brain and lymphoreticular organs such as spleen. In the latter, PrP(Sc) is thought to replicate mainly in follicular dendritic cells within spleen follicles. Although the presence of PrP(Sc) is a hallmark for prion disease and serves as a main diagnostic criterion, in certain instances the amount of PrP(Sc) does not correlate well with neurotoxicity or prion infectivity. Therefore, it has been proposed that prions might be a mixture of different conformers and aggregates with differing properties. This study investigated the impact of disruption of spleen architecture by neoplasia on the abundance of different PrP species in spleens of prion-infected mice. Although follicular integrity was completely disturbed, titres of prion infectivity in neoplastic spleens were not significantly altered, yet no protease-resistant PrP(Sc) was detectable. Instead, unique protease-sensitive prion species could be detected in neoplastic spleens. These results indicate the dissociation of PrP(Sc) and prion infectivity and showed the presence of non-PrP(Sc) PrP species in spleen with divergent biochemical properties that become apparent after tissue architecture disruption.

AB - Prion diseases are fatal neurodegenerative disorders. An important step in disease pathophysiology is the conversion of cellular prion protein (PrP(C)) to disease-associated misfolded conformers (PrP(Sc)). These misfolded PrP variants are a common component of prion infectivity and are detectable in diseased brain and lymphoreticular organs such as spleen. In the latter, PrP(Sc) is thought to replicate mainly in follicular dendritic cells within spleen follicles. Although the presence of PrP(Sc) is a hallmark for prion disease and serves as a main diagnostic criterion, in certain instances the amount of PrP(Sc) does not correlate well with neurotoxicity or prion infectivity. Therefore, it has been proposed that prions might be a mixture of different conformers and aggregates with differing properties. This study investigated the impact of disruption of spleen architecture by neoplasia on the abundance of different PrP species in spleens of prion-infected mice. Although follicular integrity was completely disturbed, titres of prion infectivity in neoplastic spleens were not significantly altered, yet no protease-resistant PrP(Sc) was detectable. Instead, unique protease-sensitive prion species could be detected in neoplastic spleens. These results indicate the dissociation of PrP(Sc) and prion infectivity and showed the presence of non-PrP(Sc) PrP species in spleen with divergent biochemical properties that become apparent after tissue architecture disruption.

KW - Animals

KW - Disease Models, Animal

KW - Mice

KW - Spleen/pathology

KW - Peptide Hydrolases/metabolism

KW - Prion Diseases/complications/pathology

KW - Prions/classification/isolation & purification/metabolism

KW - Splenic Neoplasms/complications/pathology

KW - Animals

KW - Disease Models, Animal

KW - Mice

KW - Spleen/pathology

KW - Peptide Hydrolases/metabolism

KW - Prion Diseases/complications/pathology

KW - Prions/classification/isolation & purification/metabolism

KW - Splenic Neoplasms/complications/pathology

U2 - 10.1099/vir.0.045922-0

DO - 10.1099/vir.0.045922-0

M3 - SCORING: Journal article

C2 - 23136363

VL - 94

SP - 453

EP - 463

JO - J GEN VIROL

JF - J GEN VIROL

SN - 0022-1317

IS - Pt 2

M1 - Pt 2

ER -