{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,8,4]],"date-time":"2024-08-04T04:42:54Z","timestamp":1722746574810},"reference-count":48,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2012,6,1]],"date-time":"2012-06-01T00:00:00Z","timestamp":1338508800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2012,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            We report here the transmission of human prions to 18 new transgenic (Tg) mouse lines expressing 8 unique chimeric human\/mouse prion proteins (PrP). Extracts from brains of two patients, who died of sporadic Creutzfeldt-Jakob disease (sCJD), contained either sCJD(MM1) or sCJD(VV2) prion strains and were used for inocula. Mice expressing chimeric PrP showed a direct correlation between expression level and incubation period for sCJD(MM1) prions irrespective of whether the transgene encoded methionine (M) or valine (V) at polymorphic residue 129. Tg mice expressing chimeric transgenes encoding V129 were unexpectedly resistant to infection with sCJD(VV2) prions, and when transmission did occur, it was accompanied by a change in strain type. The transmission of sCJD(MM1) prions was modulated by single amino acid reversions of each human PrP residue in the chimeric sequence. Reverting human residue 137 in the chimeric transgene from I to M prolonged the incubation time for sCJD(MM1) prions by more than 100 days; structural analyses suggest a profound change in the orientation of amino acid side chains with the I\u2192M mutation. These findings argue that changing the surface charge in this region of PrP greatly altered the interaction between PrP isoforms during prion replication. Our studies contend that strain-specified replication of prions is modulated by PrP sequence-specific interactions between the prion precursor PrP\n            <jats:sup>C<\/jats:sup>\n            and the infectious product PrP\n            <jats:sup>Sc<\/jats:sup>\n            .\n          <\/jats:p>","DOI":"10.1128\/jvi.07027-11","type":"journal-article","created":{"date-parts":[[2012,3,23]],"date-time":"2012-03-23T02:34:05Z","timestamp":1332470045000},"page":"6033-6041","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":14,"title":["Identification of I137M and Other Mutations That Modulate Incubation Periods for Two Human Prion Strains"],"prefix":"10.1128","volume":"86","author":[{"given":"Kurt","family":"Giles","sequence":"first","affiliation":[{"name":"Institute for Neurodegenerative Diseases, University of California San Francisco, San Francisco, California, USA"},{"name":"Departments of Neurology, University of 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