NR AORD
AU Casalone,C.; Zanusso,G.; Acutis,P.L.; Crescio,M.I.; Corona,C.; Ferrari,S.; Capobianco,R.; Tagliavini,F.; Monaco,S.; Caramelli,M.
TI Identification of a Novel Molecular and Neuropathological BSE Phenotype in Italy
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - DG-46
PT Konferenz-Poster
AB It is generally accepted that BSE is caused by a single, stable prion strain, since no evidence of phenotypic heterogeneity has been reported to date. Recently, we observed two BSE-affected cattle with a previously unrecognized neuropathological profile and PrPres type. This finding emerged from the analysis of the whole brain of a series of BSE cases, including six Friesian/Bruna Alpina cattle (group 1), and one Piemontese and one Bruna Alpina cattle (group 2). On immunohistochemistry, group 1 showed the typical BSE profile, with linear, glial, and granular patterns of PrP deposition, while group 2 had large PrP aggregates and amyloid plaques. This variation was paralleled by a difference in both size and glycoform ratio of PrPres on immunoblot. While group 1 showed the distinctive BSE signature with overrepresentation of the high-Mr glycoform, group 2 was marked by the predominance of the low-Mr glycoform and a PrPres fragment of lower molecular weight. The brain regional distribution of PrPres was also different in that the highest amount was detected in the brainstem and thalamus of group 1, and in the olfactory bulb, pyriform cortex and thalamus of group 2. These differences were not related to differences in the coding region of the PrP gene. Our results suggest the presence of two distinct prion strains in Italian cattle population. Transmission studies have been undertaken to asses the relevance of the "amyloidotic" form of BSE to other mammalian prion diseases, including CJD.
IN Unter 8 daraufhin untersuchten italienischen BSE-Rindern entdeckten die Autoren bei 2 Tieren - einem Piemonteser Fleischrind (http://www.aid.de/landwirtschaft/tierspecial/rinderrassen/piemont.htm) und einem Braunvieh-Rind der Rasse Bruna Alpina (http://www.inseparabile.com/bruna_alpina.htm) - ungewöhnliche neuropathologische Schädigungsmuster und Prionprotein-Glykosilierungsmuster. Verglichen mit normalen BSE-Hirnen fanden die Autoren große Prionprotein-Ablagerungen und amyloide Plaques. Im Western blot zeigten die proteaseresistenten Prionproteinfragmente dieser beiden Tiere eine reduzierte Größe und ein abweichendes Glykosilierungsmuster. Während normalerweise bei BSE die an beiden Glykosilierungsstellen glykosilierten Prionproteine dominieren, fand man bei den abweichenden Fällen besonders viel einfach glykosiliertes Prionprotein. Während normalerweise das proteaseresistente Prionprotein vor allem im Stammhirn und im Thalamus nachgewiesen wird, fand man es bei den neuartigen Fällen vor allem im Riechkolben, im Pyriformen Cortex und im Thalamus. Unterschiede in den kodierenden Regionen der Prionproteingene bestanden aber nicht. Die Autoren haben Übertragungsexperimente gestartet, um den Verdacht einer neuen BSE-Variante zu erhärten.
AD C. Casalone, P.L. Acutis, M.I. Crescio, C. Corona, M. Caramelli, CEA-Istituto Zooprofilattico di Turin; G. Zanusso, S. Ferrari, S. Monaco, Department of Neurological and Visual Sciences University of Verona, Italy; R. Capobianco, F. Tagliavini, Istituto Nazionale Neurologico Carlo Besta Milano, Italy
SP englisch
PO Deutschland
ZF kritische Zusammenfassung von Roland Heynkes