Prions of Ruminants Show Distinct Splenotropisms in an Ovine Transgenic Mouse Model 英文参考文献.docVIP

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Prions of Ruminants Show Distinct Splenotropisms in an Ovine Transgenic Mouse Model 英文参考文献.doc

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Prions of Ruminants Show Distinct Splenotropisms in an Ovine Transgenic Mouse Model 英文参考文献

PrionsofRuminantsShowDistinctSplenotropismsinan OvineTransgenicMouseModel ThierryBaron*,AnnaBencsik,EricMorignat AgenceFranc?aise deSe′curite′ SanitairedesAliments–Lyon,Unite′ ATNC,Lyon,France Abstract Background: Transmissible agents involved in prion diseases differ in their capacities to target different regions of the centralnervoussystemandlymphoidtissues,whicharealsohost-dependent. Methodology/Principal Findings:Protease-resistant prionprotein(PrPres)wasanalysedbyWesternblotinthespleen of transgenicmice(TgOvPrP4)thatexpresstheovineprionproteinunderthecontroloftheneuron-specificenolasepromoter, afterinfectionbyintra-cerebralroutewithavarietyoftransmissiblespongiformencephalopathies(TSEs)fromcattleand small ruminants. Splenic PrPres was consistently detected in classical BSE and in most natural scrapie sources, the electrophoreticpatternshowingsimilarfeaturestothatofcerebralPrPres.HoweversplenicPrPreswasnotdetectedinL-type BSE and TME-in-cattle, or in the CH1641 experimental scrapie isolate, indicating that some TSE strains showed reduced splenotropismintheovinetransgenicmice.IncontrastwithCH1641,PrPreswasalsoconsistentlydetectedinthespleenof mice infected with six natural ‘‘CH1641-like’’ scrapie isolates, but then showed clearly different molecular features from thoseidentifiedinthebrains(unglycosylatedPrPresat,18kDawithremovalofthe12B2epitope)ofovinetransgenicmice or of sheep. These features included different cleavage of the main PrPres cleavage product (unglycosylated PrPres at ,19kDa with preservation of the 12B2 epitope) and absence of the additional C-terminally cleaved PrPres product (unglycosylatedformat,14kDa)thatwasdetectedinthebrain. Conclusion/Significance: Studies in a transgenic mouse model expressing the sheep prion protein revealed different capacitiesofruminantprionstopropagateinthespleen.Theyshowedunexpectedfeaturesin‘‘CH1641-like’’ovinescrapie suggesting that such isolates contain mixed conformers with distinct capacities to propag