期刊
JOURNAL OF GENERAL VIROLOGY
卷 84, 期 -, 页码 1033-1045出版社
MICROBIOLOGY SOC
DOI: 10.1099/vir.0.18825-0
关键词
-
Scrapie and bovine spongiform encephalopathy (BSE) are transmissible spongiform encephalopathies (TSEs) or prion diseases affecting domestic and exotic ruminants. In previous immunohistochemical studies, we have shown that different sheep TSE sources may be distinguished by both the proportion of disease-specific prion protein (Prp(d)) accumulation relative to different cell types in the brain (the 'Prp(d) profile') and by different labelling patterns for PrP peptide sequences within phagocytic cells. In the present study, we have further characterized the intracellular accumulation patterns of PrPd in the lymphoreticular system (LRS) and in the brain of sheep clinically affected with scrapie or BSE. BSE-infected PrPARQ/(ARQ) sheep of different breeds were compared with scrapie-infected sheep of different PrP genotypes. Cases of BSE infection could be distinguished from scrapie cases by a marked reduction in labelling of Prpd containing the 84-105 amino acid residues in phagocytic cells of the LRS and in neurones and glia of the brain. These results therefore indicate that TSE agent-dependent processing of PrP in specific cell types within the brain and LRS can be used to distinguish between BSE in PrPARQ/ARQ sheep and scrapie in sheep of several PrP genotypes. Three different N-terminal peptide antibody labelling patterns were recognized for different cell types in different tissues of BSE-infected sheep, suggesting that different truncated forms of PrPd are formed following infections with this agent strain. These variations in the cleavage sites of BSE Prp(d) may be due to cell-specific variation in endosomal-lysosomal digestion or to cell- and tissue-specific differences in BSE Prpd conformation.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据