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Article ; Online: Short and sweet: How glycans impact prion conversion, cofactor interactions, and cross-species transmission.

Aguilar-Calvo, Patricia / Callender, Julia A / Sigurdson, Christina J

2021 Volume 17, Issue 1, Page(s) e1009123

MeSH term(s)	Amyloid/chemistry ; Amyloid/metabolism ; Animals ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; PrPC Proteins/metabolism ; Prion Diseases/metabolism ; Prion Diseases/transmission ; Prions/chemistry ; Prions/metabolism ; Species Specificity
Chemical Substances	Amyloid ; Polysaccharides ; PrPC Proteins ; Prions
Language	English
Publishing date	2021-01-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1009123
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Article ; Online: Met

Espinosa, Juan Carlos / Marín-Moreno, Alba / Aguilar-Calvo, Patricia / Torres, Juan María

Neuropathology and applied neurobiology

2020 Volume 47, Issue 4, Page(s) 506–518

Abstract: Aims: The amino acid sequence of prion protein (PrP) is a key determinant in the transmissibility of prion diseases. While PrP sequence is highly conserved among mammalian species, minor changes in the PrP amino acid sequence may confer alterations in ... ...

Abstract	Aims: The amino acid sequence of prion protein (PrP) is a key determinant in the transmissibility of prion diseases. While PrP sequence is highly conserved among mammalian species, minor changes in the PrP amino acid sequence may confer alterations in the transmissibility of prion diseases. Classical bovine spongiform encephalopathy (C-BSE) is the only zoonotic prion strain reported to date causing variant Creutzfeldt-Jacob disease (vCJD) in humans, although experimental transmission points to atypical L-BSE and some classical scrapie isolates as also zoonotic. The precise molecular elements in the human PrP sequence that limit the transmissibility of prion strains such as sheep/goat scrapie or cervid chronic wasting disease (CWD) are not well known. Methods: The transmissibility of a panel of diverse prions from different species was compared in transgenic mice expressing either wild-type human PrP Results: VDQ-HuTg372 mice were more susceptible to prions than MDE-HuTg340 mice in a strain-dependent manner. Conclusions: Met
MeSH term(s)	Amino Acids/chemistry ; Animals ; Evolution, Molecular ; Humans ; Mice, Transgenic ; Prion Diseases/physiopathology ; Prion Proteins/chemistry
Chemical Substances	Amino Acids ; Prion Proteins
Language	English
Publishing date	2020-12-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80371-6
ISSN	1365-2990 ; 0305-1846
ISSN (online)	1365-2990
ISSN	0305-1846
DOI	10.1111/nan.12676
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Article ; Online: Canine D

Marín-Moreno, Alba / Espinosa, Juan Carlos / Aguilar-Calvo, Patricia / Fernández-Borges, Natalia / Pitarch, José Luis / González, Lorenzo / Torres, Juan María

Scientific reports

2021 Volume 11, Issue 1, Page(s) 14309

Abstract: ... E/ ... ...

Abstract	E/D
MeSH term(s)	Animals ; Dogs ; Female ; Humans ; Kaplan-Meier Estimate ; Male ; Prion Diseases/genetics ; Prion Diseases/metabolism ; Prion Proteins/genetics ; Prion Proteins/metabolism ; Proportional Hazards Models ; Ruminants/microbiology ; Scrapie/microbiology ; Sheep
Chemical Substances	Prion Proteins
Language	English
Publishing date	2021-07-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-93594-x
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Article ; Online: Noninvasive Antemortem Detection of Retinal Prions by a Fluorescent Tracer.

Aguilar-Calvo, Patricia / Sevillano, Alejandro M / Rasool, Suhail / Cao, Kevin J / Randolph, Lyndsay M / Rissman, Robert A / Sarraf, Stella T / Yang, Jerry / Sigurdson, Christina J

Journal of Alzheimer's disease : JAD

2022 Volume 88, Issue 3, Page(s) 1137–1145

Abstract: Background: Neurodegenerative diseases are widespread yet challenging to diagnose and stage antemortem. As an extension of the central nervous system, the eye harbors retina ganglion cells vulnerable to degeneration, and visual symptoms are often an ... ...

Abstract	Background: Neurodegenerative diseases are widespread yet challenging to diagnose and stage antemortem. As an extension of the central nervous system, the eye harbors retina ganglion cells vulnerable to degeneration, and visual symptoms are often an early manifestation of neurodegenerative disease. Objective: Here we test whether prion protein aggregates could be detected in the eyes of live mice using an amyloid-binding fluorescent probe and high-resolution retinal microscopy. Methods: We performed retinal imaging on an experimental mouse model of prion-associated cerebral amyloid angiopathy in a longitudinal study. An amyloid-binding fluorophore was intravenously administered, and retinal imaging was performed at timepoints corresponding to early, mid-, and terminal prion disease. Retinal amyloid deposits were quantified and compared to the amyloid load in the brain. Results: We report that by early prion disease (50% timepoint), discrete fluorescent foci appeared adjacent to the optic disc. By later timepoints, the fluorescent foci surrounded the optic disc and tracked along retinal vasculature. Conclusion: The progression of perivascular amyloid can be directly monitored in the eye by live imaging, illustrating the utility of this technology for diagnosing and monitoring the progression of cerebral amyloid angiopathy.
MeSH term(s)	Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloidogenic Proteins/metabolism ; Amyloidosis ; Animals ; Cerebral Amyloid Angiopathy/metabolism ; Longitudinal Studies ; Mice ; Neurodegenerative Diseases ; Prion Diseases/diagnostic imaging ; Prion Diseases/metabolism ; Prions/metabolism ; Retina/diagnostic imaging ; Retina/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloidogenic Proteins ; Prions
Language	English
Publishing date	2022-06-29
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/JAD-220314
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Article ; Online: Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation.

Espinosa, Juan Carlos / Marín-Moreno, Alba / Aguilar-Calvo, Patricia / Benestad, Sylvie L / Andreoletti, Olivier / Torres, Juan María

The Journal of infectious diseases

2020 Volume 223, Issue 6, Page(s) 1103–1112

Abstract: Although experimental transmission of bovine spongiform encephalopathy (BSE) to pigs and transgenic mice expressing pig cellular prion protein (PrPC) (porcine PrP [PoPrP]-Tg001) has been described, no natural cases of prion diseases in pig were reported. ...

Abstract	Although experimental transmission of bovine spongiform encephalopathy (BSE) to pigs and transgenic mice expressing pig cellular prion protein (PrPC) (porcine PrP [PoPrP]-Tg001) has been described, no natural cases of prion diseases in pig were reported. This study analyzed pig-PrPC susceptibility to different prion strains using PoPrP-Tg001 mice either as animal bioassay or as substrate for protein misfolding cyclic amplification (PMCA). A panel of isolates representatives of different prion strains was selected, including classic and atypical/Nor98 scrapie, atypical-BSE, rodent scrapie, human Creutzfeldt-Jakob-disease and classic BSE from different species. Bioassay proved that PoPrP-Tg001-mice were susceptible only to the classic BSE agent, and PMCA results indicate that only classic BSE can convert pig-PrPC into scrapie-type PrP (PrPSc), independently of the species origin. Therefore, conformational flexibility constraints associated with pig-PrP would limit the number of permissible PrPSc conformations compatible with pig-PrPC, thus suggesting that pig-PrPC may constitute a paradigm of low conformational flexibility that could confer high resistance to the diversity of prion strains.
MeSH term(s)	Animals ; Brain/metabolism ; Cattle ; Encephalopathy, Bovine Spongiform/transmission ; Mice ; Mice, Transgenic ; PrPSc Proteins ; Prion Proteins ; Prions/metabolism ; Scrapie ; Swine
Chemical Substances	PrPSc Proteins ; Prion Proteins ; Prions
Language	English
Publishing date	2020-01-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiz646
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Article ; Online: Erratum to: Porcine Prion Protein as a Paradigm of Limited Susceptibility to Prion Strain Propagation.

Espinosa, Juan Carlos / Marín-Moreno, Alba / Aguilar-Calvo, Patricia / Benestad, Sylvie L / Andreoletti, Olivier / Torres, Juan María

The Journal of infectious diseases

2020 Volume 221, Issue 12, Page(s) 2085

Language	English
Publishing date	2020-03-02
Publishing country	United States
Document type	Journal Article ; Published Erratum
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiaa073
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Article ; Online: Nonpathogenic Heterologous Prions Can Interfere with Prion Infection in a Strain-Dependent Manner.

Marín-Moreno, Alba / Aguilar-Calvo, Patricia / Pitarch, José Luis / Espinosa, Juan Carlos / Torres, Juan María

Journal of virology

2018 Volume 92, Issue 24

Abstract: Co-occurrence of different prion strains into the same host has been recognized as a natural phenomenon for several sporadic Creutzfeldt-Jakob disease (sCJD) patients and natural scrapie cases. The final outcome of prion coinfection is not easily ... ...

Abstract	Co-occurrence of different prion strains into the same host has been recognized as a natural phenomenon for several sporadic Creutzfeldt-Jakob disease (sCJD) patients and natural scrapie cases. The final outcome of prion coinfection is not easily predictable. In addition to the usual factors that influence prion conversion, the replication of one strain may entail positive or negative consequences to the other. The main aim of this study was to gain insights into the prion coinfection and interference concepts and their potential therapeutic implications. Here, different mouse models were challenged with several combinations of prion strains coupled on the basis of the lengths of their incubation periods and the existence/absence of a species barrier in the tested animal model. We found that nontransmissible strains can interfere the replication of fully transmissible strains when there is a species transmission barrier involved, as happened with the combination of a mouse (22L) and a human (sCJD) strain. However, this phenomenon seems to be strain dependent, since no interference was observed when the human strain coinoculated was vCJD. For the other combinations tested in this study, the results suggest that both strains replicate independently without effect on the replication of one over the other. It is common that the strain with more favorable conditions (e.g., a higher speed of disease development or the absence of a species barrier) ends being the only one detectable at the terminal stage of the disease. However, this does not exclude the replication of the least favored strain, leading to situations of the coexistence of prion strains.
MeSH term(s)	Animals ; Brain/metabolism ; Brain/pathology ; Coinfection ; Disease Models, Animal ; Humans ; Mice ; Mice, Transgenic ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Prion Diseases/transmission ; Prions/classification ; Prions/genetics ; Prions/metabolism ; Species Specificity
Chemical Substances	Prions
Language	English
Publishing date	2018-11-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01086-18
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Zs.A 609: Show issues

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Article ; Online: Neuronal Ndst1 depletion accelerates prion protein clearance and slows neurodegeneration in prion infection.

PLoS pathogens

2023 Volume 19, Issue 9, Page(s) e1011487

Abstract: Select prion diseases are characterized by widespread cerebral plaque-like deposits of amyloid fibrils enriched in heparan sulfate (HS), a abundant extracellular matrix component. HS facilitates fibril formation in vitro, yet how HS impacts fibrillar ... ...

Abstract	Select prion diseases are characterized by widespread cerebral plaque-like deposits of amyloid fibrils enriched in heparan sulfate (HS), a abundant extracellular matrix component. HS facilitates fibril formation in vitro, yet how HS impacts fibrillar plaque growth within the brain is unclear. Here we found that prion-bound HS chains are highly sulfated, and that the sulfation is essential for accelerating prion conversion in vitro. Using conditional knockout mice to deplete the HS sulfation enzyme, Ndst1 (N-deacetylase / N-sulfotransferase) from neurons or astrocytes, we investigated how reducing HS sulfation impacts survival and prion aggregate distribution during a prion infection. Neuronal Ndst1-depleted mice survived longer and showed fewer and smaller parenchymal plaques, shorter fibrils, and increased vascular amyloid, consistent with enhanced aggregate transit toward perivascular drainage channels. The prolonged survival was strain-dependent, affecting mice infected with extracellular, plaque-forming, but not membrane bound, prions. Live PET imaging revealed rapid clearance of recombinant prion protein monomers into the CSF of neuronal Ndst1- deficient mice, neuronal, further suggesting that HS sulfate groups hinder transit of extracellular prion protein monomers. Our results directly show how a host cofactor slows the spread of prion protein through the extracellular space and identify an enzyme to target to facilitate aggregate clearance.
MeSH term(s)	Animals ; Mice ; Heparitin Sulfate/metabolism ; Mice, Knockout ; Neurons/enzymology ; Prion Diseases/metabolism ; Prion Proteins/genetics ; Prions/metabolism ; Sulfotransferases/genetics ; Sulfotransferases/metabolism
Chemical Substances	Heparitin Sulfate (9050-30-0) ; Prion Proteins ; Prions ; heparitin sulfotransferase (EC 2.8.2.8) ; Sulfotransferases (EC 2.8.2.-)
Language	English
Publishing date	2023-09-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1011487
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Article ; Online: Thermostability as a highly dependent prion strain feature.

Marín-Moreno, Alba / Aguilar-Calvo, Patricia / Moudjou, Mohammed / Espinosa, Juan Carlos / Béringue, Vincent / Torres, Juan María

Scientific reports

2019 Volume 9, Issue 1, Page(s) 11396

Abstract: Prion diseases are caused by the conversion of physiological ... ...

Abstract	Prion diseases are caused by the conversion of physiological PrP
MeSH term(s)	Animals ; Brain/pathology ; Disease Models, Animal ; Endopeptidase K/metabolism ; Hot Temperature/adverse effects ; Humans ; Mice ; Mice, Transgenic ; PrPC Proteins/metabolism ; PrPSc Proteins/metabolism ; PrPSc Proteins/pathogenicity ; Prion Diseases/pathology ; Protein Folding ; Protein Stability ; Proteolysis
Chemical Substances	PrPC Proteins ; PrPSc Proteins ; Endopeptidase K (EC 3.4.21.64)
Language	English
Publishing date	2019-08-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-019-47781-6
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Article ; Online: Diminished Neuronal ESCRT-0 Function Exacerbates AMPA Receptor Derangement and Accelerates Prion-Induced Neurodegeneration.

The Journal of neuroscience : the official journal of the Society for Neuroscience

2023 Volume 43, Issue 21, Page(s) 3970–3984

Abstract: Endolysosomal defects in neurons are central to the pathogenesis of prion and other neurodegenerative disorders. In prion disease, prion oligomers traffic through the multivesicular body (MVB) and are routed for degradation in lysosomes or for release in ...

Abstract	Endolysosomal defects in neurons are central to the pathogenesis of prion and other neurodegenerative disorders. In prion disease, prion oligomers traffic through the multivesicular body (MVB) and are routed for degradation in lysosomes or for release in exosomes, yet how prions impact proteostatic pathways is unclear. We found that prion-affected human and mouse brain showed a marked reduction in Hrs and STAM1 (ESCRT-0), which route ubiquitinated membrane proteins from early endosomes into MVBs. To determine how the reduction in ESCRT-0 impacts prion conversion and cellular toxicity
MeSH term(s)	Male ; Female ; Mice ; Humans ; Animals ; Prions/metabolism ; Prion Proteins/metabolism ; Receptors, AMPA/metabolism ; Neurons/metabolism ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Neurodegenerative Diseases/metabolism ; Endosomal Sorting Complexes Required for Transport/metabolism
Chemical Substances	Prions ; Prion Proteins ; Receptors, AMPA ; Endosomal Sorting Complexes Required for Transport
Language	English
Publishing date	2023-04-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.1878-22.2023
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