Glycans are not necessary to maintain the pathobiological features of bovine spongiform encephalopathy
2022
Otero, Alicia | Barrio, Tomás | Eraña, Hasier | Charco, Jorge | Betancor, Marina | Díaz-Domínguez, Carlos | Marín, Belén | Andréoletti, Olivier | Torres, Juan | Kong, Qingzhong | Badiola, Juan | Bolea, Rosa | Castilla, Joaquín | Universidad de Zaragoza = University of Zaragoza [Saragossa University] = Université de Saragosse | Centro de Encefalopatías y Enfermedades Transmisibles Emergentes ; Universidad de Zaragoza = University of Zaragoza [Saragossa University] = Université de Saragosse | Interactions hôtes-agents pathogènes [Toulouse] (IHAP) ; Ecole Nationale Vétérinaire de Toulouse (ENVT) ; Institut National Polytechnique (Toulouse) (Toulouse INP) ; Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National Polytechnique (Toulouse) (Toulouse INP) ; Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) | Center for Cooperative Research in Biosciences = Centro de Investigación cooperativa en biociencia (Derio, Biscay, Espagne) (CIC bioGUNE) | Basque Research and Technology Alliance (BRTA) | Université de Montréal (UdeM) | Case Western Reserve University [Cleveland] | National Prion Disease Pathology Surveillance Center ; Case Western Reserve University [Cleveland] | Ikerbasque - Basque Foundation for Science | Centro de Investigación Biomédica en Red de Enfermedades Infecciosas (CIBERINFEC)
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Show more [+] Less [-]English. The role of the glycosylation status of PrP C in the conversion to its pathological counterpart and on cross-species transmission of prion strains has been widely discussed. 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 C . Bovine, ovine and porcine-passaged BSE, and variant Creutzfeldt-Jakob disease (vCJD) isolates were used as seeds/inocula in both in vitro and in vivo propagation assays using the non-glycosylated human PrP C -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 in vitro 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 C is not essential for the preservation of the human transmission barrier for BSE prions or for the maintenance of BSE strain properties.
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