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3. Large-scale validation of skin prion seeding activity as a biomarker for diagnosis of prion diseases

Author

Zhang, Weiguanliu, Orrú, Christina D., Foutz, Aaron, Ding, Mingxuan, Yuan, Jue, Shah, Syed Zahid Ali, Zhang, Jing, Kotobelli, Keisi, Gerasimenko, Maria, Gilliland, Tricia, Chen, Wei, Tang, Michelle, Cohen, Mark, Safar, Jiri, Xu, Bin, Hong, Dao-Jun, Cui, Li, Hughson, Andrew G., Schonberger, Lawrence B., Tatsuoka, Curtis, Chen, Shu G., Greenlee, Justin J., Wang, Zerui, Appleby, Brian S., Caughey, Byron, and Zou, Wen-Quan

Published
2024
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6. Shortening heparan sulfate chains prolongs survival and reduces parenchymal plaques in prion disease caused by mobile, ADAM10-cleaved prions

Author

Aguilar-Calvo, Patricia, Sevillano, Alejandro M, Bapat, Jaidev, Soldau, Katrin, Sandoval, Daniel R, Altmeppen, Hermann C, Linsenmeier, Luise, Pizzo, Donald P, Geschwind, Michael D, Sanchez, Henry, Appleby, Brian S, Cohen, Mark L, Safar, Jiri G, Edland, Steven D, Glatzel, Markus, Nilsson, K Peter R, Esko, Jeffrey D, and Sigurdson, Christina J

Subjects
Biomedical and Clinical Sciences, Neurosciences, Neurodegenerative, Infectious Diseases, Brain Disorders, Emerging Infectious Diseases, Rare Diseases, Transmissible Spongiform Encephalopathy (TSE), 2.1 Biological and endogenous factors, Aetiology, Neurological, ADAM10 Protein, Animals, Brain, Heparitin Sulfate, Humans, Mice, Prion Diseases, Prions, Amyloid, Neurodegeneration, Glycosaminoglycans, ADAM10 cleavage, Clinical Sciences, Neurology & Neurosurgery
Abstract

Cofactors are essential for driving recombinant prion protein into pathogenic conformers. Polyanions promote prion aggregation in vitro, yet the cofactors that modulate prion assembly in vivo remain largely unknown. Here we report that the endogenous glycosaminoglycan, heparan sulfate (HS), impacts prion propagation kinetics and deposition sites in the brain. Exostosin-1 haploinsufficient (Ext1+/-) mice, which produce short HS chains, show a prolonged survival and a redistribution of plaques from the parenchyma to vessels when infected with fibrillar prions, and a modest delay when infected with subfibrillar prions. Notably, the fibrillar, plaque-forming prions are composed of ADAM10-cleaved prion protein lacking a glycosylphosphatidylinositol anchor, indicating that these prions are mobile and assemble extracellularly. By analyzing the prion-bound HS using liquid chromatography-mass spectrometry (LC-MS), we identified the disaccharide signature of HS differentially bound to fibrillar compared to subfibrillar prions, and found approximately 20-fold more HS bound to the fibrils. Finally, LC-MS of prion-bound HS from human patients with familial and sporadic prion disease also showed distinct HS signatures and higher HS levels associated with fibrillar prions. This study provides the first in vivo evidence of an endogenous cofactor that accelerates prion disease progression and enhances parenchymal deposition of ADAM10-cleaved, mobile prions.

Published
2020

7. Prion Seeds Distribute throughout the Eyes of Sporadic Creutzfeldt-Jakob Disease Patients

Author

Orrù, Christina D, Soldau, Katrin, Cordano, Christian, Llibre-Guerra, Jorge, Green, Ari J, Sanchez, Henry, Groveman, Bradley R, Edland, Steven D, Safar, Jiri G, Lin, Jonathan H, Caughey, Byron, Geschwind, Michael D, Sigurdson, Christina J, Supattapone, Surachai, and Zerr, Inga

Subjects
Neurosciences, Emerging Infectious Diseases, Rare Diseases, Brain Disorders, Transmissible Spongiform Encephalopathy (TSE), Infectious Diseases, Neurodegenerative, Eye Disease and Disorders of Vision, Aetiology, 2.1 Biological and endogenous factors, Eye, Neurological, Aged, Autopsy, Brain, Creutzfeldt-Jakob Syndrome, Female, Humans, Immunohistochemistry, Male, Middle Aged, Prion Diseases, Prions, Retina, Creutzfeldt-Jakob disease, RT-QuIC, eye, prion, Microbiology
Abstract

Sporadic Creutzfeldt-Jakob disease (sCJD) is the most common prion disease in humans and has been iatrogenically transmitted through corneal graft transplantation. Approximately 40% of sCJD patients develop visual or oculomotor symptoms and may seek ophthalmological consultation. Here we used the highly sensitive real-time quaking-induced conversion (RT-QuIC) assay to measure postmortem prion seeding activities in cornea, lens, ocular fluid, retina, choroid, sclera, optic nerve, and extraocular muscle in the largest series of sCJD patient eyes studied by any assay to date. We detected prion seeding activity in 100% of sCJD eyes, representing three common sCJD subtypes, with levels varying by up to 4 log-fold among individuals. The retina consistently showed the highest seed levels, which in some cases were only slightly lower than brain. Within the retina, prion deposits were detected by immunohistochemistry (IHC) in the retinal outer plexiform layer in most sCJD cases, and in some eyes the inner plexiform layer, consistent with synaptic prion deposition. Prions were not detected by IHC in any other eye region. With RT-QuIC, prion seed levels generally declined in eye tissues with increased distance from the brain, and yet all corneas had prion seeds detectable. Prion seeds were also present in the optic nerve, extraocular muscle, choroid, lens, vitreous, and sclera. Collectively, these results reveal that sCJD patients accumulate prion seeds throughout the eye, indicating the potential diagnostic utility as well as a possible biohazard.IMPORTANCE Cases of iatrogenic prion disease have been reported from corneal transplants, yet the distribution and levels of prions throughout the eye remain unknown. This study probes the occurrence, level, and distribution of prions in the eyes of patients with sporadic Creutzfeldt-Jakob disease (sCJD). We tested the largest series of prion-infected eyes reported to date using an ultrasensitive technique to establish the prion seed levels in eight regions of the eye. All 11 cases had detectable prion seeds in the eye, and in some cases, the seed levels in the retina approached those in brain. In most cases, prion deposits could also be seen by immunohistochemical staining of retinal tissue; other ocular tissues were negative. Our results have implications for estimating the risk for iatrogenic transmission of sCJD as well as for the development of antemortem diagnostic tests for prion diseases.

Published
2018

9. Genome wide association study of clinical duration and age at onset of sporadic CJD

Author

Hummerich, Holger, Speedy, Helen, Campbell, Tracy, Darwent, Lee, Hill, Elizabeth, Collins, Steven, Stehmann, Christiane, Kovacs, Gabor G., Geschwind, Michael D., Frontzek, Karl, Budka, Herbert, Gelpi, Ellen, Aguzzi, Adriano, van der Lee, Sven J., van Duijn, Cornelia M., Liberski, Pawel P., Calero, Miguel, Sanchez-Juan, Pascual, Bouaziz-Amar, Elodie, Laplanche, Jean Louis, Haïk, Stéphane, Brandel, Jean Phillipe, Mammana, Angela, Capellari, Sabina, Poleggi, Anna, Ladogana, Anna, Pocchiari, Maurizio, Zafar, Saima, Booth, Stephanie, Jansen, Gerard H., Areškevičiūtė, Aušrinė, Lund, Eva Løbner, Glisic, Katie, Parchi, Piero, Hermann, Peter, Zerr, Inga, Appleby, Brian S., Safar, Jiri, Gambetti, Pierluigi, Collinge, John, Mead, Simon, Hummerich, Holger, Speedy, Helen, Campbell, Tracy, Darwent, Lee, Hill, Elizabeth, Collins, Steven, Stehmann, Christiane, Kovacs, Gabor G., Geschwind, Michael D., Frontzek, Karl, Budka, Herbert, Gelpi, Ellen, Aguzzi, Adriano, van der Lee, Sven J., van Duijn, Cornelia M., Liberski, Pawel P., Calero, Miguel, Sanchez-Juan, Pascual, Bouaziz-Amar, Elodie, Laplanche, Jean Louis, Haïk, Stéphane, Brandel, Jean Phillipe, Mammana, Angela, Capellari, Sabina, Poleggi, Anna, Ladogana, Anna, Pocchiari, Maurizio, Zafar, Saima, Booth, Stephanie, Jansen, Gerard H., Areškevičiūtė, Aušrinė, Lund, Eva Løbner, Glisic, Katie, Parchi, Piero, Hermann, Peter, Zerr, Inga, Appleby, Brian S., Safar, Jiri, Gambetti, Pierluigi, Collinge, John, and Mead, Simon

Abstract

Human prion diseases are rare, transmissible and often rapidly progressive dementias. The most common type, sporadic Creutzfeldt-Jakob disease (sCJD), is highly variable in clinical duration and age at onset. Genetic determinants of late onset or slower progression might suggest new targets for research and therapeutics. We assembled and array genotyped sCJD cases diagnosed in life or at autopsy. Clinical duration (median:4, interquartile range (IQR):2.5–9 (months)) was available in 3,773 and age at onset (median:67, IQR:61–73 (years)) in 3,767 cases. Phenotypes were successfully transformed to approximate normal distributions allowing genome-wide analysis without statistical inflation. 53 SNPs achieved genome-wide significance for the clinical duration phenotype; all of which were located at chromosome 20 (top SNP rs1799990, pvalue = 3.45x10-36, beta = 0.34 for an additive model; rs1799990, pvalue = 9.92x10-67, beta = 0.84 for a heterozygous model). Fine mapping, conditional and expression analysis suggests that the well-known non-synonymous variant at codon 129 is the obvious outstanding genome-wide determinant of clinical duration. Pathway analysis and suggestive loci are described. No genome-wide significant SNP determinants of age at onset were found, but the HS6ST3 gene was significant (pvalue = 1.93 x 10−6) in a gene-based test. We found no evidence of genome-wide genetic correlation between case-control (disease risk factors) and case-only (determinants of phenotypes) studies. Relative to other common genetic variants, PRNP codon 129 is by far the outstanding modifier of CJD survival suggesting only modest or rare variant effects at other genetic loci.

Published
2024

10. Identification of novel risk loci and causal insights for sporadic Creutzfeldt-Jakob disease: a genome-wide association study

Author

Jones, Emma, Hummerich, Holger, Viré, Emmanuelle, Uphill, James, Dimitriadis, Athanasios, Speedy, Helen, Campbell, Tracy, Norsworthy, Penny, Quinn, Liam, Whitfield, Jerome, Linehan, Jacqueline, Jaunmuktane, Zane, Brandner, Sebastian, Jat, Parmjit, Nihat, Akin, How Mok, Tze, Ahmed, Parvin, Collins, Steven, Stehmann, Christiane, Sarros, Shannon, Kovacs, Gabor G, Geschwind, Michael D, Golubjatnikov, Aili, Frontzek, Karl, Budka, Herbert, Aguzzi, Adriano, Karamujić-Čomić, Hata, van der Lee, Sven J, Ibrahim-Verbaas, Carla A, van Duijn, Cornelia M, Sikorska, Beata, Golanska, Ewa, Liberski, Pawel P, Calero, Miguel, Calero, Olga, Sanchez-Juan, Pascual, Salas, Antonio, Martinón-Torres, Federico, Bouaziz-Amar, Elodie, Haïk, Stéphane, Laplanche, Jean-Louis, Brandel, Jean-Phillipe, Amouyel, Phillipe, Lambert, Jean-Charles, Parchi, Piero, Bartoletti-Stella, Anna, Capellari, Sabina, Poleggi, Anna, Ladogana, Anna, Pocchiari, Maurizio, Aneli, Serena, Matullo, Giuseppe, Knight, Richard, Zafar, Saima, Zerr, Inga, Booth, Stephanie, Coulthart, Michael B, Jansen, Gerard H, Glisic, Katie, Blevins, Janis, Gambetti, Pierluigi, Safar, Jiri, Appleby, Brian, Collinge, John, and Mead, Simon

Published
2020
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14. Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT-P301L mutation

Author

Daude, Nathalie, Kim, Chae, Kang, Sang-Gyun, Eskandari-Sedighi, Ghazaleh, Haldiman, Tracy, Yang, Jing, Fleck, Shelaine C., Gomez-Cardona, Erik, Han, Zhuang Zhuang, Borrego-Ecija, Sergi, Wohlgemuth, Serene, Julien, Olivier, Wille, Holger, Molina-Porcel, Laura, Gelpi, Ellen, Safar, Jiri G., and Westaway, David

Published
2020
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19. Conserved properties of human and bovine prion strains on transmission to guinea pigs

Author

Safar, Jiri G, Giles, Kurt, Lessard, Pierre, Letessier, Frederic, Patel, Smita, Serban, Ana, DeArmond, Stephen J, and Prusiner, Stanley B

Subjects
Biomedical and Clinical Sciences, Clinical Sciences, Foodborne Illness, Rare Diseases, Transmissible Spongiform Encephalopathy (TSE), Neurodegenerative, Emerging Infectious Diseases, Neurosciences, Brain Disorders, Infectious Diseases, Aetiology, 2.1 Biological and endogenous factors, Neurological, Amino Acid Sequence, Animals, Blotting, Western, Cattle, Guinea Pigs, Humans, Mice, Mice, Transgenic, Molecular Sequence Data, Prion Diseases, Sequence Homology, Amino Acid, BSE, GSS, guinea pig, prions, sCJD, vCJD, Pathology, Clinical sciences
Abstract

The first transmissions of human prion diseases to rodents used guinea pigs (Gps, Cavia porcellus). Later, transgenic mice expressing human or chimeric human/mouse PrP replaced Gps, but the small size of the mouse limits some investigations. To investigate the fidelity of strain-specific prion transmission to Gps, we inoculated 'type 1' and 'type 2' prion strains into Gps, and we measured the incubation times and determined the strain-specified size of the unglycosylated, protease-resistant (r) PrP(Sc) fragment. Prions passaged once in Gps from cases of sporadic (s) Creutzfeldt-Jakob disease (CJD) and Gerstmann-Sträussler-Scheinker (GSS) disease caused by the P102L mutation were used, as well as human prions from a variant (v) CJD case, bovine prions from bovine spongiform encephalopathy (BSE) and mouse-passaged scrapie prions. Variant CJD and BSE prions transmitted to all the inoculated Gps with incubation times of 367 ± 4 and 436 ± 28 days, respectively. On second passage in Gps, vCJD and BSE prions caused disease in 287 ± 4 and 310 ± 4 days, whereas sCJD and GSS prions transmitted in 237 ± 4 and 279 ± 19 days, respectively. Although hamster Sc237 prions transmitted to two of three Gps after 574 and 792 days, mouse-passaged RML and 301V prion strains, the latter derived from BSE prions, failed to transmit disease to Gps. Those Gps inoculated with vCJD or BSE prions exhibited 'type 2' unglycosylated, rPrP(Sc) (19 kDa), whereas those receiving sCJD or GSS prions displayed 'type 1' prions (21 kDa), as determined by western blotting. Such strain-specific properties were maintained in Gps as well as mice expressing a chimeric human/mouse transgene. Gps may prove particularly useful in further studies of novel human prions such as those causing vCJD.

Published
2011

20. Diagnosis of Human Prion Disease

Author

Safar, Jiri G., Geschwind, Michael D., Deering, Camille, Didorenko, Svetlana, Sattavat, Mamta, Sanchez, Henry, Serban, Ana, Vey, Martin, Baron, Henry, Giles, Kurt, Miller, Bruce L., DeArmond, Stephen J., and Prusiner, Stanley B.

Published
2005

21. Prion proteins in subpopulations of white blood cells from patients with sporadic Creutzfeldt–Jakob disease

Author

Choi, Ed M, Geschwind, Michael D, Deering, Camille, Pomeroy, Kristen, Kuo, Amy, Miller, Bruce L, Safar, Jiri G, and Prusiner, Stanley B

Subjects
Biomedical and Clinical Sciences, Immunology, Acquired Cognitive Impairment, Clinical Research, Infectious Diseases, Neurodegenerative, Emerging Infectious Diseases, Rare Diseases, Neurosciences, Transmissible Spongiform Encephalopathy (TSE), Brain Disorders, Aetiology, 2.1 Biological and endogenous factors, Neurological, Aged, Aged, 80 and over, Blood Platelets, Creutzfeldt-Jakob Syndrome, Female, Humans, Leukocytes, Male, Middle Aged, PrPC Proteins, PrPSc Proteins, Protein Isoforms, assay, blood, Creutzfeldt-Jakob disease, detection, prion, WBC, Clinical Sciences, Pathology, Clinical sciences
Abstract

Recent cases of prion transmission in humans following transfusions using blood donated by patients with asymptomatic variant Creutzfeldt-Jakob disease (CJD) implicate the presence of prion infectivity in peripheral blood. In this study, we examined the levels of the normal, cellular prion protein (PrPC), and the disease-causing isoform (PrPSc) in subpopulations of circulating white blood cells (WBCs) from patients with sporadic (s) CJD, age-matched neurological controls and healthy donors. Though widely distributed, the highest levels of PrPC were found in a subpopulation of T lymphocytes: approximately 12,000 PrPC molecules were found per CD4+CD45RA-CD62L- effector memory T helper cell. Although platelets expressed low levels of PrPC on their surface, their high abundance in circulation resulted in the majority of PrPC being platelet associated. Using quantitative fluorescence-activated cell sorting analysis, we found that neither WBC composition nor the amount of cell-surface PrPC molecules was altered in patients with sCJD. Eight different WBC fraction types from the peripheral blood of patients with sCJD were assessed for PrPSc. We were unable to find any evidence for PrPSc in purified granulocytes, monocytes, B cells, CD4+ T cells, CD8+ T cells, natural killer cells, nonclassical gamma delta T cells, or platelets. If human WBCs harbor prion infectivity in patients with sCJD, then the levels are likely to be low.

Published
2009

25. Autoantibodies against the prion protein in individuals with PRNP mutations

Author

Frontzek, Karl, Carta, Manfredi, Losa, Marco, Epskamp, Mirka, Meisl, Georg, Anane, Alice, Brandel, Jean-Philippe, Camenisch, Ulrike, Castilla, Joaquín, Haïk, Stéphane, Knowles, Tuomas, Lindner, Ewald, Lutterotti, Andreas, Minikel, Eric Vallabh, Roiter, Ignazio, Safar, Jiri G., Sanchez-Valle, Raquel, Žáková, Dana, Hornemann, Simone, and Aguzzi, Adriano

Published
2020
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26. Mutant PrPSc conformers induced by a synthetic peptide and several prion strains

Author

Tremblay, Patrick, Ball, Haydn L, Kaneko, Kiyotoshi, Groth, Darlene, Hegde, Ramanujan S, Cohen, Fred E, DeArmond, Stephen J, Prusiner, Stanley B, and Safar, Jiri G

Abstract

Gerstmann-Strfiussier-Scheinker (GSS) disease is a dominantly inherited, human prion disease caused by a mutation in the prion protein (PrP) gene. One mutation causing GSS is P102L, denoted P101L in mouse PrP (MoPrP). In a line of transgenic mice denoted Tg2866, the P101L mutation in MoPrP produced neurodegeneration when expressed at high levels. MoPrPSc(P101L) was detected both by the conformation-dependent immunoassay and after protease digestion at 4degreesC. Transmission of prions from the brains of Tg2866 mice to those of Tg196 mice expressing low levels of MoPrP(P101L) was accompanied by accumulation of protease-resistant MoPrPsc(P101L) that had previously escaped detection due to its low concentration. This conformer exhibited characteristics similar to those found in brain tissue from GSS patients. Earlier, we demonstrated that a synthetic peptide harboring the P101L mutation and folded into a beta-rich conformation initiates GSS in Tg196 mice (29). Here we report that this peptide-induced disease can be serially passaged in Tg196 mice and that the PrP conformers accompanying disease progression are conformationally indistinguishable from MoPrPSc(P101L) found in Tg2866 mice developing spontaneous prion disease. In contrast to GSS prions, the 301V, RML, and 139A prion strains produced large amounts of protease-resistant PrPSc in the brains of Tg196 mice. Our results argue that MoPrPSc(P101L) may exist in at least several different conformations, each of which is biologically active. Such conformations occurred spontaneously in Tg2866 mice expressing high levels of MoPrPC(P10IL) as well as in Tg196 mice expressing low levels of MoPrPC(P101L) that were inoculated with brain extracts from ill Tg2866 mice, with a synthetic peptide with the P101L mutation and folded into a beta-rich structure, or with prions recovered from sheep with scrapie or cattle with bovine spongiform encephalopathy.

Published
2004

27. Correction to: Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT‑P301L mutation

Author

Daude, Nathalie, Kim, Chae, Kang, Sang‑Gyun, Eskandari‑Sedighi, Ghazaleh, Haldiman, Tracy, Yang, Jing, Fleck, Shelaine C., Gomez‑Cardona, Erik, Han, Zhuang Zhuang, Borrego‑Ecija, Sergi, Wohlgemuth, Serene, Julien, Olivier, Wille, Holger, Molina‑Porcel, Laura, Gelpi, Ellen, Safar, Jiri G., and Westaway, David

Published
2021
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28. Age at onset in genetic prion disease and the design of preventive clinical trials

Author

Minikel, Eric Vallabh, Vallabh, Sonia M., Orseth, Margaret C., Brandel, Jean-Philippe, Haïk, Stéphane, Laplanche, Jean-Louis, Zerr, Inga, Parchi, Piero, Capellari, Sabina, Safar, Jiri, Kenny, Janna, Fong, Jamie C., Takada, Leonel T., Ponto, Claudia, Hermann, Peter, Knipper, Tobias, Stehmann, Christiane, Kitamoto, Tetsuyuki, Ae, Ryusuke, Hamaguchi, Tsuyoshi, Sanjo, Nobuo, Tsukamoto, Tadashi, Mizusawa, Hidehiro, Collins, Steven J., Chiesa, Roberto, Roiter, Ignazio, de Pedro-Cuesta, Jesús, Calero, Miguel, Geschwind, Michael D., Yamada, Masahito, Nakamura, Yosikazu, and Mead, Simon

Published
2019
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30. Large-Scale Validation of Skin Prion Seeding Activity as a Biomarker for Postmortem Diagnosis of Creutzfeldt-Jakob Disease

Author

Zhang, Weiguanliu, primary, Orrú, Christina D., additional, Foutz, Aaron, additional, Ding, Mingxuan, additional, Yuan, Jue, additional, Shah, Syed Zahid Ali, additional, Zhang, Jing, additional, Kotobelli, Keisi, additional, Gerasimenko, Maria, additional, Gilliland, Tricia, additional, Chen, Wei, additional, Tang, Michelle, additional, Cohen, Mark, additional, Safar, Jiri, additional, Hong, Dao-Jun, additional, Cui, Li, additional, Hughson, Andrew G., additional, Schonberger, Lawrence, additional, Tatsuoka, Curtis, additional, Chen, Shu G., additional, Greenlee, Justin, additional, Wang, Zerui, additional, Appleby, Brian S., additional, Caughey, Byron, additional, and Zou, Wenquan, additional

Published
2023
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33. Prion seeding activity and infectivity in skin samples from patients with sporadic Creutzfeldt-Jakob disease

Author

Orrú, Christina D., Yuan, Jue, Appleby, Brian S., Li, Baiya, Li, Yu, Winner, Dane, Wang, Zerui, Zhan, Yi-An, Rodgers, Mark, Rarick, Jason, Wyza, Robert E., Joshi, Tripti, Wang, Gong-Xian, Cohen, Mark L., Zhang, Shulin, Groveman, Bradley R., Petersen, Robert B., Ironside, James W., Quiñones-Mateu, Miguel E., Safar, Jiri G., Kong, Qingzhong, Caughey, Byron, and Zou, Wen-Quan

Published
2017
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50. Human Prions and Plasma Lipoproteins

Author

Safar, Jiri G., Wille, Holger, Geschwind, Michael D., Deering, Camille, Latawiec, Diane, Serban, Ana, King, David J., Legname, Giuseppe, Weisgraber, Karl H., Mahley, Robert W., Miller, Bruce L., DeArmond, Stephen J., and Prusiner, Stanley B.

Published
2006
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