Abstract
Prions are transmissible agents that comprised of a misfolded protein PrPSc that is posttranslationally derived from the normal isoform PrPC. Prion strains are operationally defined by differences in the distribution and intensity of spongiform degeneration and distribution of PrPSc in the CNS. The mechanism by which prion strains are encoded is not known; however, current evidence suggests that the conformation of PrPSc encodes prion strain diversity. In natural prion disease, more than one prion strain can exist in an individual. Prion strains, when present in the same host, can interfere with each other, a process that may be important during prion adaptation following interspecies transmission. While the parameters that influence prion strain interference are beginning to be described, the mechanism responsible for strain interference is not known.
| Original language | English |
|---|---|
| Title of host publication | Volume 1, Physiology and Pathophysiology |
| Publisher | Springer New York |
| Pages | 193-204 |
| Number of pages | 12 |
| Volume | 1 |
| ISBN (Electronic) | 9781461453055 |
| ISBN (Print) | 1461453046, 9781461453048 |
| DOIs | |
| State | Published - Nov 1 2013 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Medicine(all)
- Neuroscience(all)
Cite this
Prion strain interference. / Schutt, Charles R.; Shikiya, Ronald A.; Bartz, Jason C.
Volume 1, Physiology and Pathophysiology. Vol. 1 Springer New York, 2013. p. 193-204.Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Prion strain interference
AU - Schutt, Charles R.
AU - Shikiya, Ronald A.
AU - Bartz, Jason C.
PY - 2013/11/1
Y1 - 2013/11/1
N2 - Prions are transmissible agents that comprised of a misfolded protein PrPSc that is posttranslationally derived from the normal isoform PrPC. Prion strains are operationally defined by differences in the distribution and intensity of spongiform degeneration and distribution of PrPSc in the CNS. The mechanism by which prion strains are encoded is not known; however, current evidence suggests that the conformation of PrPSc encodes prion strain diversity. In natural prion disease, more than one prion strain can exist in an individual. Prion strains, when present in the same host, can interfere with each other, a process that may be important during prion adaptation following interspecies transmission. While the parameters that influence prion strain interference are beginning to be described, the mechanism responsible for strain interference is not known.
AB - Prions are transmissible agents that comprised of a misfolded protein PrPSc that is posttranslationally derived from the normal isoform PrPC. Prion strains are operationally defined by differences in the distribution and intensity of spongiform degeneration and distribution of PrPSc in the CNS. The mechanism by which prion strains are encoded is not known; however, current evidence suggests that the conformation of PrPSc encodes prion strain diversity. In natural prion disease, more than one prion strain can exist in an individual. Prion strains, when present in the same host, can interfere with each other, a process that may be important during prion adaptation following interspecies transmission. While the parameters that influence prion strain interference are beginning to be described, the mechanism responsible for strain interference is not known.
UR - http://www.scopus.com/inward/record.url?scp=84929528444&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84929528444&partnerID=8YFLogxK
U2 - 10.1007/978-1-4614-5305-5_14
DO - 10.1007/978-1-4614-5305-5_14
M3 - Chapter
AN - SCOPUS:84929528444
SN - 1461453046
SN - 9781461453048
VL - 1
SP - 193
EP - 204
BT - Volume 1, Physiology and Pathophysiology
PB - Springer New York
ER -