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Here, we assessed the effect on strain characteristics of bovine spongiform encephalopathy (BSE) isolates with different transmission histories upon propagation on a model expressing a non-glycosylated human PrP<jats:sup>C<\/jats:sup>. Bovine, ovine and porcine-passaged BSE, and variant Creutzfeldt-Jakob disease (vCJD) isolates were used as seeds\/inocula in both <jats:italic>in vitro<\/jats:italic> and <jats:italic>in vivo<\/jats:italic> propagation assays using the non-glycosylated human PrP<jats:sup>C<\/jats:sup>-expressing mouse model (TgNN6h). After protein misfolding cyclic amplification (PMCA), all isolates maintained the biochemical characteristics of BSE. On bioassay, all PMCA-propagated BSE prions were readily transmitted to TgNN6h mice, in agreement with our previous <jats:italic>in vitro<\/jats:italic> results. TgNN6h mice reproduced the characteristic neuropathological and biochemical hallmarks of BSE, suggesting that the absence of glycans did not alter the pathobiological features of BSE prions. Moreover, back-passage of TgNN6h-adapted BSE prions to BoTg110 mice recovered the full BSE phenotype, confirming that the glycosylation of human PrP<jats:sup>C<\/jats:sup> is not essential for the preservation of the human transmission barrier for BSE prions or for the maintenance of BSE strain properties.<\/jats:p>","DOI":"10.1371\/journal.ppat.1010900","type":"journal-article","created":{"date-parts":[[2022,10,7]],"date-time":"2022-10-07T17:43:27Z","timestamp":1665164607000},"page":"e1010900","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":3,"title":["Glycans are not necessary to maintain the pathobiological features of bovine spongiform 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