In:
PLOS Pathogens, Public Library of Science (PLoS), Vol. 18, No. 10 ( 2022-10-7), p. e1010900-
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
1553-7374
DOI:
10.1371/journal.ppat.1010900
DOI:
10.1371/journal.ppat.1010900.g001
DOI:
10.1371/journal.ppat.1010900.g002
DOI:
10.1371/journal.ppat.1010900.g003
DOI:
10.1371/journal.ppat.1010900.g004
DOI:
10.1371/journal.ppat.1010900.g005
DOI:
10.1371/journal.ppat.1010900.g006
DOI:
10.1371/journal.ppat.1010900.t001
DOI:
10.1371/journal.ppat.1010900.t002
DOI:
10.1371/journal.ppat.1010900.s001
DOI:
10.1371/journal.ppat.1010900.s002
DOI:
10.1371/journal.ppat.1010900.s003
DOI:
10.1371/journal.ppat.1010900.s004
DOI:
10.1371/journal.ppat.1010900.s005
DOI:
10.1371/journal.ppat.1010900.r001
DOI:
10.1371/journal.ppat.1010900.r002
DOI:
10.1371/journal.ppat.1010900.r003
DOI:
10.1371/journal.ppat.1010900.r004
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2022
detail.hit.zdb_id:
2205412-1
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