Year: 2009
Type: article
Abstract: Transmissible spongiform encephalopathy (TSE) diseases are known to cross species barriers, but the pathologic and biochemical changes that occur during transmission are not well understood. To better understand these changes, we infected 6 hamster species with 263K hamster scrapie strain and, after each of 3 successive passages in the new species, analyzed abnormal proteinase K (PK)-resistant prion protein (PrPres) glycoform ratios, PrPres PK sensitivity, incubation periods, and lesion profiles. Unique 263K molecular and biochemical profiles evolved in each of the infected hamster species. Characteristics of 263K in the new hamster species seemed to correlate best with host factors rather than agent strain. Furthermore, 2 polymorphic regions of the prion protein amino acid sequence correlated with profile differences in these TSE-infected hamster species.
Source: Emerging infectious diseases
Authors: Kimberly D. Meade-White, Kent D. Barbian, Brent Race, Cynthia Favara, Don Gardner, Lara Taubner, Stephen Porcella, Richard Race
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: diamond
Funder: National Institutes of Health
OpenAlex ID: W2134996189