{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T06:55:13Z","timestamp":1790232913441,"version":"4.1.0"},"reference-count":41,"publisher":"Society for Neuroscience","issue":"3","license":[{"start":{"date-parts":[[2014,7,15]],"date-time":"2014-07-15T00:00:00Z","timestamp":1405382400000},"content-version":"vor","delay-in-days":181,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-sa\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Neurosci."],"published-print":{"date-parts":[[2014,1,15]]},"abstract":"<jats:p>Zoonotic prion transmission was reported after the bovine spongiform encephalopathy (BSE) epidemic, when &gt;200 cases of prion disease in humans were diagnosed as variant Creutzfeldt-Jakob disease. Assessing the risk of cross-species prion transmission remains challenging. We and others have studied how specific amino acid residue differences between species impact prion conversion and have found that the \u03b22-\u03b12 loop region of the mouse prion protein (residues 165\u2013175) markedly influences infection by sheep scrapie, BSE, mouse-adapted scrapie, deer chronic wasting disease, and hamster-adapted scrapie prions. The tyrosine residue at position 169 is strictly conserved among mammals and an aromatic side chain in this position is essential to maintain a 3<jats:sub>10<\/jats:sub>-helical turn in the \u03b22-\u03b12 loop. Here we examined the impact of the Y169G substitution together with the previously described S170N, N174T \u201crigid loop\u201d substitutions on cross-species prion transmission<jats:italic>in vivo<\/jats:italic>and<jats:italic>in vitro<\/jats:italic>. We found that transgenic mice expressing mouse PrP containing the triple-amino acid substitution completely resisted infection with two strains of mouse prions and with deer chronic wasting disease prions. These studies indicate that Y169 is important for prion formation, and they provide a strong indication that variation of the \u03b22-\u03b12 loop structure can modulate interspecies prion transmission.<\/jats:p>","DOI":"10.1523\/jneurosci.4636-13.2014","type":"journal-article","created":{"date-parts":[[2014,1,15]],"date-time":"2014-01-15T18:11:24Z","timestamp":1389809484000},"page":"1022-1027","source":"Crossref","is-referenced-by-count":80,"title":["Prion Transmission Prevented by Modifying the \u03b22-\u03b12 Loop Structure of Host PrP<sup>C<\/sup>"],"prefix":"10.1523","volume":"34","author":[{"given":"Timothy 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