<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>106(12)</volume><submitter>van Keulen LJ</submitter><pubmed_abstract>Two cases of atypical scrapie (AS) from Dutch sheep were passaged to WT mice and ovine and bovine prion protein (PrP) transgenic mice. Both AS isolates failed to transmit to WT mice but were successfully transmitted to ovine PrP transgenic Tg338 and Tg59 mice, carrying two different sheep PrP alleles. Western blot analysis of the brains from both mouse lines showed a similar protease-resistant band of ~6-8 kDa, which corresponded to the amino acids ~93-155 of the ovine PrP. Sagittal and coronal immunohistochemical profiles of the abnormal scrapie-associated PrP (PrP&lt;sup>Sc&lt;/sup>) in the mouse brain were constructed and revealed that PrP&lt;sup>Sc&lt;/sup> was mainly located in white matter structures in the frontal parts of the brain. Cross-passages between the Tg338 and Tg59 mice showed that th</pubmed_abstract><journal>The Journal of general virology</journal><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12723909</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Co-presence of classical scrapie but not classical Bovine Spongiform Encephalopathy in transmissions from Dutch sheep with atypical scrapie.</pubmed_title><pmcid>PMC12723909</pmcid><pubmed_authors>Bossers-de Vries R</pubmed_authors><pubmed_authors>van Keulen LJ</pubmed_authors><pubmed_authors>Dolstra CH</pubmed_authors><pubmed_authors>Bossers A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Co-presence of classical scrapie but not classical Bovine Spongiform Encephalopathy in transmissions from Dutch sheep with atypical scrapie.</name><description>Two cases of atypical scrapie (AS) from Dutch sheep were passaged to WT mice and ovine and bovine prion protein (PrP) transgenic mice. Both AS isolates failed to transmit to WT mice but were successfully transmitted to ovine PrP transgenic Tg338 and Tg59 mice, carrying two different sheep PrP alleles. Western blot analysis of the brains from both mouse lines showed a similar protease-resistant band of ~6-8 kDa, which corresponded to the amino acids ~93-155 of the ovine PrP. Sagittal and coronal immunohistochemical profiles of the abnormal scrapie-associated PrP (PrP&lt;sup>Sc&lt;/sup>) in the mouse brain were constructed and revealed that PrP&lt;sup>Sc&lt;/sup> was mainly located in white matter structures in the frontal parts of the brain. Cross-passages between the Tg338 and Tg59 mice showed that th</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Dec</publication><modification>2026-06-07T05:22:17.215Z</modification><creation>2026-06-07T03:06:24.351Z</creation></dates><accession>S-EPMC12723909</accession><cross_references><pubmed>41432060</pubmed><doi>10.1099/jgv.0.002202</doi></cross_references></HashMap>