Abstract
Prion diseases affect a wide range of mammal species and are caused by a misfolded selfpropagating isoform (PrPSc) of the normal prion protein (PrPC). Distinct strains of prions exist and are operationally defined by differences in a heritable phenotype under controlled experimental transmission conditions. Prion strains can differ in incubation period, clinical signs of disease, tissue tropism, and host range. The mechanism by which a protein-only pathogen can encode strain diversity is only beginning to be understood. The prevailing hypothesis is that prion strain diversity is encoded by strain-specific conformations of PrPSc; however, strain-specific cellular cofactors have been identified in vitro that may also contribute to prion strain diversity. Although much progress has been made on understanding the etiological agent of prion disease, the relationship between the strain-specific properties of PrPSc and the resulting phenotype of disease in animals is poorly understood.
| Original language | English (US) |
|---|---|
| Article number | a024349 |
| Journal | Cold Spring Harbor perspectives in medicine |
| Volume | 6 |
| Issue number | 12 |
| DOIs | |
| State | Published - 2016 |
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All Science Journal Classification (ASJC) codes
- Medicine(all)
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Prion strain diversity. / Bartz, Jason C.
In: Cold Spring Harbor perspectives in medicine, Vol. 6, No. 12, a024349, 2016.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Prion strain diversity
AU - Bartz, Jason C.
PY - 2016
Y1 - 2016
N2 - Prion diseases affect a wide range of mammal species and are caused by a misfolded selfpropagating isoform (PrPSc) of the normal prion protein (PrPC). Distinct strains of prions exist and are operationally defined by differences in a heritable phenotype under controlled experimental transmission conditions. Prion strains can differ in incubation period, clinical signs of disease, tissue tropism, and host range. The mechanism by which a protein-only pathogen can encode strain diversity is only beginning to be understood. The prevailing hypothesis is that prion strain diversity is encoded by strain-specific conformations of PrPSc; however, strain-specific cellular cofactors have been identified in vitro that may also contribute to prion strain diversity. Although much progress has been made on understanding the etiological agent of prion disease, the relationship between the strain-specific properties of PrPSc and the resulting phenotype of disease in animals is poorly understood.
AB - Prion diseases affect a wide range of mammal species and are caused by a misfolded selfpropagating isoform (PrPSc) of the normal prion protein (PrPC). Distinct strains of prions exist and are operationally defined by differences in a heritable phenotype under controlled experimental transmission conditions. Prion strains can differ in incubation period, clinical signs of disease, tissue tropism, and host range. The mechanism by which a protein-only pathogen can encode strain diversity is only beginning to be understood. The prevailing hypothesis is that prion strain diversity is encoded by strain-specific conformations of PrPSc; however, strain-specific cellular cofactors have been identified in vitro that may also contribute to prion strain diversity. Although much progress has been made on understanding the etiological agent of prion disease, the relationship between the strain-specific properties of PrPSc and the resulting phenotype of disease in animals is poorly understood.
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UR - http://www.scopus.com/inward/citedby.url?scp=85006043284&partnerID=8YFLogxK
U2 - 10.1101/cshperspect.a024349
DO - 10.1101/cshperspect.a024349
M3 - Article
VL - 6
JO - Cold Spring Harbor perspectives in medicine
JF - Cold Spring Harbor perspectives in medicine
SN - 2157-1422
IS - 12
M1 - a024349
ER -