Variable Protease-Sensitive Prionopathy Transmission to Bank Voles

Nonno, Romolo; Notari, Silvio; Di Bari, Michele Angelo; Cali, Ignazio; Pirisinu, Laura; d’Agostino, Claudia; Cracco, Laura; Kofskey, Diane; Vanni, Ilaria; Lavrich, Jody; Parchi, Piero; Agrimi, Umberto; Gambetti, Pierluigi

i

Variable Protease-Sensitive Prionopathy Transmission to Bank Voles

Supporting Files

January 2019
By Nonno, Romolo ; Notari, Silvio ; Di Bari, Michele Angelo ; ...

File Language:

English

Details

Alternative Title:

Emerg Infect Dis
Personal Author:

Nonno, Romolo ; Notari, Silvio ; Di Bari, Michele Angelo ; Cali, Ignazio ; Pirisinu, Laura ; d’Agostino, Claudia ; Cracco, Laura ; Kofskey, Diane ; Vanni, Ilaria ; Lavrich, Jody ; Parchi, Piero ; Agrimi, Umberto ; Gambetti, Pierluigi
Description:

Variably protease-sensitive prionopathy (VPSPr), a recently described human sporadic prion disease, features a protease-resistant, disease-related prion protein (resPrP|) displaying 5 fragments reminiscent of Gerstmann-Sträussler-Scheinker disease. Experimental VPSPr transmission to human PrP-expressing transgenic mice, although replication of the VPSPr resPrP| profile succeeded, has been incomplete because of second passage failure. We bioassayed VPSPr in bank voles, which are susceptible to human prion strains. Transmission was complete; first-passage attack rates were 5%-35%, and second-passage rates reached 100% and survival times were 50% shorter. We observed 3 distinct phenotypes and resPrP| profiles; 2 imitated sporadic Creutzfeldt-Jakob disease resPrP|, and 1 resembled Gerstmann-Sträussler-Scheinker disease resPrPD. The first 2 phenotypes may be related to the presence of minor PrP| components in VPSPr. Full VPSPr transmission confirms permissiveness of bank voles to human prions and suggests that bank vole PrP may efficiently reveal an underrepresented native strain but does not replicate the complex VPSPr PrP| profile.
Subjects:

Animals Arvicolinae Brain Disease Models, Animal Genotype Gerstmann-Straussler-Scheinker Disease Humans Mice Mice, Transgenic Peptide Hydrolases Phenotype Prion Diseases Prions Protein Isoforms Research
Source:

Emerg Infect Dis. 25(1):73-81
Pubmed ID:

30561322
Pubmed Central ID:

PMC6302590
Document Type:

Journal Article
Funding:

P01 AI106705/AI/NIAID NIH HHS/United States ; R01 NS083687/NS/NINDS NIH HHS/United States
Volume:

25
Issue:

1
Collection(s):

Emerging Infectious Diseases
Main Document Checksum:

urn:sha256:043e3edb8d49a9df139fc76b360325f7cb16763b4ab9d81e72e208817a61474e
Download URL:

https://stacks.cdc.gov/view/cdc/80444/cdc_80444_DS1.pdf
File Type:

[PDF - 1.88 MB ]

File Language:

English

ON THIS PAGE

Details Supporting Files

CDC STACKS serves as an archival repository of CDC-published products including scientific findings, journal articles, guidelines, recommendations, or other public health information authored or co-authored by CDC or funded partners.

As a repository, CDC STACKS retains documents in their original published format to ensure public access to scientific information.