{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T23:07:11Z","timestamp":1791328031539,"version":"4.3.1"},"reference-count":46,"publisher":"American Society for Microbiology","issue":"23","license":[{"start":{"date-parts":[[2016,12,1]],"date-time":"2016-12-01T00:00:00Z","timestamp":1480550400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"name":"Alliance Biosecure","award":["BoHuToHu"],"award-info":[{"award-number":["BoHuToHu"]}]},{"name":"Institut National de Veille Sanitaire","award":["CNR ATNC"],"award-info":[{"award-number":["CNR ATNC"]}]},{"DOI":"10.13039\/501100002915","name":"Fondation pour la Recherche M\u00e9dicale","doi-asserted-by":"publisher","award":["Equipe FRM DEQ20150331689"],"award-info":[{"award-number":["Equipe FRM DEQ20150331689"]}],"id":[{"id":"10.13039\/501100002915","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2016,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Prions are proteinaceous pathogens responsible for subacute spongiform encephalopathies in animals and humans. The prions responsible for bovine spongiform encephalopathy (BSE) are zoonotic agents, causing variant Creutzfeldt-Jakob disease (CJD) in humans. The transfer of prions between species is limited by a species barrier, which is thought to reflect structural incompatibilities between the host cellular prion protein (PrP<jats:sup>C<\/jats:sup>) and the infecting pathological PrP assemblies (PrP<jats:sup>Sc<\/jats:sup>) constituting the prion. A BSE strain variant, designated L-BSE and responsible for atypical, supposedly spontaneous forms of prion diseases in aged cattle, demonstrates zoonotic potential, as evidenced by its capacity to propagate more easily than classical BSE in transgenic mice expressing human PrP<jats:sup>C<\/jats:sup>and in nonhuman primates. In humanized mice, L-BSE propagates without any apparent species barrier and shares similar biochemical PrP<jats:sup>Sc<\/jats:sup>signatures with the CJD subtype designated MM2-cortical, thus opening the possibility that certain CJD cases classified as sporadic may actually originate from L-type BSE cross-transmission. To address this issue, we compared the biological properties of L-BSE and those of a panel of CJD subtypes representative of the human prion strain diversity using standard strain-typing criteria in human PrP transgenic mice. We found no evidence that L-BSE causes a known form of sporadic CJD.<\/jats:p><jats:p><jats:bold>IMPORTANCE<\/jats:bold>Since the quasi-extinction of classical BSE, atypical BSE forms are the sole BSE variants circulating in cattle worldwide. They are observed in rare cases of old cattle, making them difficult to detect. Extrapolation of our results suggests that L-BSE may propagate in humans as an unrecognized form of CJD, and we urge both the continued utilization of precautionary measures to eliminate these agents from the human food chain and active surveillance for CJD phenotypes in the general population.<\/jats:p>","DOI":"10.1128\/jvi.01383-16","type":"journal-article","created":{"date-parts":[[2016,9,29]],"date-time":"2016-09-29T02:49:40Z","timestamp":1475117380000},"page":"10867-10874","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":39,"title":["Absence of Evidence for a Causal Link between Bovine Spongiform Encephalopathy Strain Variant L-BSE and Known Forms of Sporadic Creutzfeldt-Jakob Disease in Human PrP Transgenic Mice"],"prefix":"10.1128","volume":"90","author":[{"given":"Emilie","family":"Jaumain","sequence":"first","affiliation":[{"name":"VIM, INRA, Universit\u00e9 Paris-Saclay, Jouy-en-Josas, 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