Prion [JOURNAL]
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Prion · 2026 Dec · PMID 42271170 · Full text
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Early diagnosis of a case of Heidenhain variant of Creutzfeld-Jakob disease by cerebrospinal fluid real-time quaking-induced conversion test.
Li L, Yan R, Wang J … +1 more , Guo Y
Prion · 2026 Dec · PMID 41894154 · Full text
Sporadic Creutzfeldt-Jakob disease (sCJD) is a rare, rapidly progressive, and fatal neurodegenerative disorder caused by the accumulation of abnormal prion proteins in the central nervous system. The Heidenhain variant (...
Sporadic Creutzfeldt-Jakob disease (sCJD) is a rare, rapidly progressive, and fatal neurodegenerative disorder caused by the accumulation of abnormal prion proteins in the central nervous system. The Heidenhain variant (HvCJD), a rare subtype of sCJD, is characterized by prominent visual symptoms at onset. Diagnosing sCJD remains challenging due to non-specific clinical presentations and the limited sensitivity and specificity of conventional tests such as magnetic resonance imaging (MRI), electroencephalography (EEG), and cerebrospinal fluid (CSF) 14-3-3 protein analysis. Recently, real-time quaking-induced conversion (RT-QuIC) has emerged as a valuable tool for improving diagnostic accuracy. We present the case of a 65-year-old man who initially experienced blurred vision and diplopia, followed by rapidly progressive dementia and dysuria. Brain MRI revealed cortical diffusion-weighted imaging (DWI) hyperintensities in the right temporo-occipital region. While his CSF 14-3-3 protein test was negative, RT-QuIC assay returned positive, leading to a final diagnosis of probable CJD. The patient died 8 weeks after diagnosis. This case highlights that HvCJD is a rare but important clinical variant in which conventional CSF 14-3-3 testing may be negative, particularly early in the disease course. In contrast, RT-QuIC demonstrates high sensitivity and specificity and can significantly aid in the early and accurate diagnosis of CJD.
Maternal chronic wasting disease infection restricts fetal head size in white-tailed deer ().
Mori J, Perez-Girones SV, Latif T … +5 more , Rivera N, Skinner D, Schlichting P, Novakofski J, Mateus-Pinilla N
Prion · 2026 Dec · PMID 41772888 · Full text
Chronic wasting disease (CWD) is a fatal neurodegenerative prion disease of cervids that can be transmitted through direct physical contact, indirect contact with a contaminated environment, or vertical transmission. CWD...
Chronic wasting disease (CWD) is a fatal neurodegenerative prion disease of cervids that can be transmitted through direct physical contact, indirect contact with a contaminated environment, or vertical transmission. CWD is characterized by a long incubation period followed by symptoms like loss of appetite resulting from the destruction of brain tissue. While the consequences for infected animals are clear, a previous study from our laboratory showing lower body weights in the foetuses of CWD-positive female deer suggests those consequences may be intergenerational. In this study, we addressed the impact of maternal CWD infection on foetal head development (as a proxy for brain growth) in wild white-tailed deer using data from CWD management efforts in northern Illinois, U.S.A. Multivariate, multilevel, Bayesian Gamma regression found that maternal CWD infection reduced foetal head nose-occipital length and crown-jaw circumference by 6.76% and frontal-occipital length by 11.31%. These findings suggest impeded brain development in the offspring of CWD-infected female deer, which could reduce fawns' survival and success after birth and lead to a decline in population fitness over time. This study is the first to demonstrate the detrimental effects of a prion disease on foetal brain development in any animal species regardless of whether vertical transmission has occurred.
Plaque-type dura mater graft-associated Creutzfeldt-Jakob disease: an autopsied case report.
Tahara D, Yokoi D, Tahara N … +7 more , Akagi A, Riku Y, Sone J, Miyahara H, Watanabe H, Katsuno M, Iwasaki Y
Prion · 2026 Dec · PMID 41762037 · Full text
Clinicopathologically, dura mater graft-associated Creutzfeldt-Jakob disease (dCJD) presents as either a non-plaque or plaque type. Here, we report an autopsy case of plaque-type dCJD, supported by genetic and biochemica...
Clinicopathologically, dura mater graft-associated Creutzfeldt-Jakob disease (dCJD) presents as either a non-plaque or plaque type. Here, we report an autopsy case of plaque-type dCJD, supported by genetic and biochemical analyses. A 41-year-old man manifested right-hand paraesthesia. He had received a dural graft in the right parietal region following a traumatic acute subdural haematoma 27 years before symptom onset. The clinical course was slowly progressive. The patient became unable to walk independently 17 months after onset, showed cognitive decline at 22 months, and developed myoclonus and akinetic mutism at 24 months. Periodic sharp-wave complexes were never observed on electroencephalography throughout the disease course. He died 26 months after symptom onset. No mutations were identified in the prion protein (PrP) gene, and the codon 129 polymorphism was homozygous for methionine. Neuropathologically, mild to moderate spongiform changes with fine vacuoles, neuronal loss, and astrogliosis were observed in the brain and spinal cord. Degeneration was relatively severe in the limbic system, striatum, thalamus, and cerebellum, resembling the distribution pattern of VV2 sporadic CJD. Abnormal PrP deposition was broadly distributed consisting of synaptic, perineuronal, and plaque forms. In particular, intense PrP staining was observed throughout the spinal grey matter. Western blotting detected intermediate-type PrP in the brain and cervical cord, but not in systemic organs. Considering the clinical course and PrP staining in the spinal cord, PrP transmission is suggested to occur not directly from the transplanted dura mater to the central nervous system, but rather indirectly via a peripheral route.
Efficient induction of motor neuron disease in transgenic G93A SOD1 mice by prion-like seeding.
Xu G, Lopez A, Brkic S … +3 more , Fromholt S, Chakrabarty P, Borchelt DR
Prion · 2026 Dec · PMID 41702846 · Full text
Mutations in superoxide dismutase 1 (SOD1) cause paralysis in familial amyotrophic lateral sclerosis and promote its misfolding into neurotoxic aggregates. Previous studies have shown that mice expressing the ALS-causing...
Mutations in superoxide dismutase 1 (SOD1) cause paralysis in familial amyotrophic lateral sclerosis and promote its misfolding into neurotoxic aggregates. Previous studies have shown that mice expressing the ALS-causing G85R variant of SOD1 develop paralysis much faster after intraspinal injection of spinal homogenates from paralysed G85R SOD1 mice. These findings, and other studies in cell models, established the prionoid templating properties of misfolded mutant SOD1. Previously, however, we noted that the widely used Gur1-G93A SOD1 mice, which express at high levels and develop paralysis by 6 months of age, were resistant to seeding by homogenates from paralysed G93A mice. A line of G93A mice that expresses at very low levels (VLE-G93A) was responsive to seeding but at low efficiency. The poor susceptibility of G93A-SOD1 mice to seeding was not what we expected if prion-like propagation is essential to SOD1 ALS pathogenesis. In our prior studies, seeding homogenates from paralysed G93A-SOD1 mice were injected into the spine of newborn mice, leading us to question whether older G93A SOD1 mice might be more susceptible to seeding. Here, we establish that adult VLE G93A SOD1 mice (up to 12 months of age) injected intrathecally with seeding homogenates containing misfolded G93A or G85R SOD1 developed accelerated motor neuron disease efficiently. Thus, we demonstrate that both the route and age of inoculation can influence the efficiency of SOD1 seeding to induce motor neuron disease in VLE G93A-SOD1 mice. These data, together with our earlier reports, suggest that prion-like templating contributes to disease progression in SOD1-ALS.
Prion 2025: advancing the understanding and treatment of prion diseases in dialogue with patients and families.
Vieira TCRG, Silva JL
Prion · 2026 Feb · PMID 41634946 · Publisher ↗
Prion 2025, held in Armação dos Búzios, Brazil (3-7 November 2025), was the first PRION congress in Latin America and brought together 260 participants from 22 countries. Building on the broadening scope of recent meetin...
Prion 2025, held in Armação dos Búzios, Brazil (3-7 November 2025), was the first PRION congress in Latin America and brought together 260 participants from 22 countries. Building on the broadening scope of recent meetings, this edition placed the cellular prion protein (PrP) back at centre stage while maintaining a strong focus on prion-like mechanisms and functional amyloids. Clinical and epidemiological sessions addressed rapidly progressive dementias and prion and prion-like diseases, underscoring the need for structured diagnostic pathways and closer interaction between surveillance networks and specialized centres. Basic science sessions explored PrP biology, with an emphasis on liquid - liquid-phase separation, early misfolding events, and structural features that underpin prion propagation and strain diversity. The programme also dedicated space to emerging diagnostics and biomarkers, as well as to therapeutic strategies, including PrP-lowering approaches and targeting proteostasis and cellular clearance pathways. Sessions on yeast, bacterial, and memory amyloids broadened the discussion to functional and evolutionary aspects of amyloid formation. Finally, Prion 2025 strengthened engagement with patient organizations and families, incorporating dedicated panels and family-oriented activities into the programme. Overall, the meeting reinforced links between basic and translational prion research and placed patients' and families' perspectives at the heart of the discussion.
Prion seeding activity in DNA extractions: implications for laboratory biosafety.
Gresch SC, Morrill T, Ellis-Cramer M … +8 more , Arifin M, Frank LE, Bartz JC, Schwabenlander MD, Wolf TM, Mitchell GB, Guan J, Larsen PA
Prion · 2026 Dec · PMID 41609668 · Full text
Infectious prions (PrP) are largely resistant to proteolytic digestion, including proteinase K (PK) digestion. While nucleic acid extracts are generally considered non-infectious from a classical microbiology context (i....
Infectious prions (PrP) are largely resistant to proteolytic digestion, including proteinase K (PK) digestion. While nucleic acid extracts are generally considered non-infectious from a classical microbiology context (i.e. free of intact bacteria and viruses), we investigated whether standard DNA purification methods co-purify PrP, posing an unrecognized biosafety risk. Commercial DNA extraction kits can eliminate conventional pathogens but are likely ineffective against PrP due to resistance to kit reagents and enzymatic degradation. Two laboratories, the University of Minnesota Center for Prion Research and Outreach (MNPRO) and the Canadian Food Inspection Agency (CFIA), independently tested filter-based and magnetic bead-based DNA extraction kits using tissues from chronic wasting disease (CWD)-positive and -negative white-tailed deer (WTD; ), as well as prion-infected and control Syrian hamster () brains. CFIA used two filter-based kits (one automated, one manual), while MNPRO tested two manual kits (filter- and magnetic bead-based). PrP seeding activity was measured in extracted DNA and source tissues using real-time quaking-induced conversion (RT-QuIC). MNPRO found substantial to almost perfect agreement between RT-QuIC seeding activity of DNA eluates from both extraction methods and that of the source WTD tissue homogenate. CFIA optimized RT-QuIC to a 30-hour runtime, achieving 74% sensitivity and 94% specificity in 88 archived WTD DNA samples. Both laboratories concluded that commercial DNA extraction kits do not eliminate PrP, enabling carry-over into DNA eluates. Until infectivity is resolved by animal bioassay, DNA from PrP-positive tissues should be handled under biosafety protocols appropriate for the originating prion disease, with decontamination and containment procedures.
Development of a user guide to support administration of the MRC Prion Disease Rating Scale in research and clinical settings for prion diseases.
Pulido RS, Marshall C, Smith AV … +8 more , Edge H, Yarlas A, Appleby B, Brandel JP, Collins S, Omer N, Zerr I, Mead S
Prion · 2025 Dec · PMID 41025622 · Full text
BACKGROUND: The prion diseases (PrD) are a group of progressive, fatal, neurodegenerative diseases, for which the Medical Research Council Prion Disease Rating Scale (MRC Scale) can be used to assess patients' functional...
BACKGROUND: The prion diseases (PrD) are a group of progressive, fatal, neurodegenerative diseases, for which the Medical Research Council Prion Disease Rating Scale (MRC Scale) can be used to assess patients' functional deterioration. Findings from previous qualitative interviews with caregivers and clinical experts identified potential ambiguities in the scale that could lead to inconsistent scoring within and/or between raters. METHODS: A draft User Guide was developed based on findings from a previous qualitative study. The draft included clarifications regarding domain wording, scoring levels, and guidance for response option selection. Five clinical experts with PrD management experience provided written feedback on the draft User Guide, which was incorporated into a revised User Guide. A 90-minute consensus meeting was then held with these experts to confirm the final content to be included in the User Guide. RESULTS: The final User Guide was designed to accompany the MRC Scale and assist with rater decisions related to which response option most accurately describes a patient's health status. Conclusions: The User Guide is expected to be a valuable complement to the MRC Scale, which is poised to rise in use and prominence as global clinical research efforts accelerate to address the significant unmet need of PrD patients.
Differential pathology of P102L-associated Gerstmann-Stäussler-Scheinker disease: exclusive presence of 8-kDa protease-resistant prion protein vs. co-existence of 8-kDa and type-1 protease-resistant prion protein, with a focus on codon 129 polymorphism.
Noguchi H, Yoshimura M, Watanabe A … +10 more , Koyama S, Sakurada N, Shijo M, Kanemaru T, Kai K, Aishima S, Koike H, Tsuboi Y, Sasagasako N, Honda H
Prion · 2025 Dec · PMID 40958206 · Full text
Gerstmann - Sträussler - Scheinker disease (GSS) is a hereditary prion disease characterized by clinicopathological heterogeneity. In Japan, the most common mutation is P102L, typically associated with prion protein (PrP...
Gerstmann - Sträussler - Scheinker disease (GSS) is a hereditary prion disease characterized by clinicopathological heterogeneity. In Japan, the most common mutation is P102L, typically associated with prion protein (PrP) plaques, spongiform changes, and synaptic PrP deposits. Two major protease-resistant PrP (PrP) types occur: type-1 PrP (21 kDa) and 8-kDa PrP. The codon 129 polymorphism (methionine or valine) influences disease phenotype, but factors underlying exclusive 8-kDa PrP expression remain unclear. We analysed two sibling P102L GSS cases exclusively exhibiting 8-kDa PrP (Case 1: 129 MM, haplotype: P102L-129 M, treated with pentosan polysulfate; Case 2: 129 MV, haplotype: P102L-129 M, treated with quinacrine hydrochloride and quinine hydrochloride) and four P102L-129 MM GSS cases exhibiting type-1 and 8-kDa PrP (Cases 3-6) to elucidate the clinicopathological effect of 8-kDa PrP and codon 129 polymorphisms. Case 1 predominantly exhibited amyloidogenic PrP plaques; Case 2 exhibited non-amyloidogenic cotton-wool PrP plaques, with minimal synaptic PrP deposits. Despite prolonged survival ( > 20 years), spongiform degeneration and neuronal loss were mild. Cases 3-6 showed numerous amyloidogenic PrP plaques, moderate-to-severe synaptic PrP deposits, and significant tissue damage. Homoeostatic microglial markers were preserved in Cases 1 and 2 but absent in Cases 3-6. Cotton-wool PrP plaques lacked amyloid cores and were associated with 8-kDa PrP and codon 129 V from the normal allele. Tissue damage was mild in P102L GSS cases exhibiting 8-kDa PrP, suggesting lower pathogenicity. Cotton-wool PrP plaque formation likely involves 8-kDa PrP and codon 129 V. Further large-scale studies are warranted to elucidate these mechanisms.
Canadian 2021 H-type Bovine Spongiform Encephalopathy case associated with a novel E211K polymorphism in prion protein gene.
Tahir W, Dudas S, Anderson R … +5 more , Yang J, Bogart S, Santiago-Mateo K, Fang Y, Quaghebeur R
Prion · 2025 Dec · PMID 40757654 · Full text
Bovine Spongiform Encephalopathy (BSE) is a fatal neurodegenerative disease in cattle which can be either classical BSE (C-BSE) or atypical BSE (including H-BSE and L-BSE). Here, we report the results of our analyses of...
Bovine Spongiform Encephalopathy (BSE) is a fatal neurodegenerative disease in cattle which can be either classical BSE (C-BSE) or atypical BSE (including H-BSE and L-BSE). Here, we report the results of our analyses of an H-BSE case found in Canada in 2021, indicating restriction of the pathological agent (PrP) mainly to the central nervous system with no or occasional weak involvement of peripheral tissues. Importantly, a non-synonymous mutation at codon 211 of the gene was detected and confirmed to be present as a germline mutation. This is the first case of BSE in Canada with a predisposing E211K mutation.
Impact of low testing numbers on chronic wasting disease apparent prevalence.
Mori JJ, Rivera NA, Brown WM … +4 more , Skinner DJ, Schlichting PE, Novakofski JE, Mateus-Pinilla NE
Prion · 2025 Dec · PMID 40641213 · Full text
Chronic wasting disease (CWD) is a fatal, neurodegenerative disease of cervids, and its management heavily relies on diagnostic testing. Test results are commonly used to calculate 'apparent prevalence' (AP) - the percen...
Chronic wasting disease (CWD) is a fatal, neurodegenerative disease of cervids, and its management heavily relies on diagnostic testing. Test results are commonly used to calculate 'apparent prevalence' (AP) - the percent of animals tested for CWD (CWD tests) with CWD-positive test results (CWD cases) - but this obscures how tests and cases individually contribute to this statistic. This is most relevant when CWD testing is limited because when few animals are tested, detection of even a single infected deer can result in a high AP that poorly reflects reality. We hypothesized that when CWD testing is limited, AP is negatively driven by testing - rather than cases - with more tests corresponding to lower APs. Graphed CWD surveillance data from townships in Illinois and Wisconsin, USA, indicate that CWD AP values ≥50% were only observed when <23 deer were tested. We used Bayesian multilevel zero-inflated Beta regression to model AP as a function of CWD tests, CWD cases and nonlinear transformations of these two terms separately for each state. The best-fit models of both identified a statistically significant negative relationship between AP and testing numbers that was modified by a positive nonlinear test covariate. This means adding tests when testing is low can have a big impact on decreasing the AP, but this relationship weakens as testing increases. We urge treating apparent prevalences ≥50% with caution and emphasize the importance of increasing the test results when initial surveillance has yielded <23 tests.
Addressing chronic wasting disease in Korean farms: topsoil removal and 2N NaOH treatment before cervid restocking.
Park KJ, Park HC, Lee YR … +4 more , Roh IS, Mitchell G, Choi YP, Sohn HJ
Prion · 2025 Dec · PMID 40625035 · Full text
Chronic wasting disease (CWD) is a highly contagious prion disease occurring in free-ranging and farmed cervids. In the Republic of Korea, cases of CWD continue to be detected almost annually, on both new and occasionall...
Chronic wasting disease (CWD) is a highly contagious prion disease occurring in free-ranging and farmed cervids. In the Republic of Korea, cases of CWD continue to be detected almost annually, on both new and occasionally previously infected farms. CWD-infected animals contaminate soil and other environmental components by shedding prions through their excreta. Since shed prions remain infectious for years in the environment, they can act as infectivity reservoirs facilitating horizontal transmission of CWD. To prevent the further spread of CWD and allow farms to resume operations, control measures on infected farms, including topsoil removal and thorough environmental treatment with 2N NaOH, have been implemented in the Republic of Korea. Restocking remediated farms with cervids was permitted after confirming the absence of prion seeding activity in soil samples using protein misfolding cyclic amplification (PMCA). A total of 215 samples from 18 remediated farms were collected and analysed using PMCA, with only 3 samples from 3 farms displaying prion seeding activity. While the disease control measures effectively eliminated prion seeding activity in CWD-affected farms, CWD recurred at two of the 18 remediated farms 4 to 5 years after restocking animals. It remains unclear whether the recurrence of CWD at the two farms was due to residual prions in the environment after the control measures, or the introduction of the infected animals from other farms. This uncertainty is heightened by the annual occurrence of CWD at multiple farms and the absence of a traceability system for farmed cervids.
Detection of chronic wasting disease prions in soil at an illegal white-tailed deer carcass disposal site.
Grunklee MK, Lichtenberg SS, Lurndahl NA … +7 more , Schwabenlander MD, Karwan DL, Li EA, Bartz JC, Yuan Q, Larsen PA, Wolf TM
Prion · 2025 Dec · PMID 40480951 · Full text
Chronic wasting disease (CWD) is a contagious prion disorder affecting cervids such as deer, elk, caribou, and moose, causing progressive and severe neurological degeneration followed by eventual death. As CWD prions (Pr...
Chronic wasting disease (CWD) is a contagious prion disorder affecting cervids such as deer, elk, caribou, and moose, causing progressive and severe neurological degeneration followed by eventual death. As CWD prions (PrP) accumulate in the body, they are shed through excreta and secreta, as well as through decomposing carcasses. Prions can persist in the environment for years, posing significant concerns for ongoing transmission to susceptible cervids and pose an unknown risk to sympatric species. We used a validated protocol for real-time quaking-induced conversion (RT-QuIC) prion amplification assay to detect prions in soil collected within and around an illegal white-tailed deer (, WTD) carcass disposal site and associated captive WTD farm in Beltrami County, Minnesota. We detected PrP in 26 of 201 soil samples across 15 locations within the illegal disposal site and one on the farm that housed the cervids. Importantly, a subset of RT-QuIC positive soil samples was collected from soils where carcasses were recovered, providing direct evidence that environmental contamination resulted from this illegal activity. These findings reveal that improper cervid carcass disposal practices may have important implications for ongoing CWD transmission through the environment.
Prion 2024 conference: from two decades of growth to a new journey forward.
Kong Y, Huang P, Shi Q … +6 more , Wang Y, Li M, Ma J, Dong XP, Hong D, Zou WQ
Prion · 2025 Dec · PMID 40459970 · Full text
The Prion 2024 annual conference, held in Nanchang, China, from 23 to 27 October, drew nearly 300 leading scientists, clinicians, researchers, and students from 17 countries to examine the latest advancements in prion re...
The Prion 2024 annual conference, held in Nanchang, China, from 23 to 27 October, drew nearly 300 leading scientists, clinicians, researchers, and students from 17 countries to examine the latest advancements in prion research and related diseases. This landmark event marked the inaugural international prion conference hosted in a developing nation for the first time and celebrated the 20th anniversary of the NeuroPrion Association, the organizing body of this prestigious annual gathering - '.' The conference spotlighted key themes such as epidemiology, pathogenesis, the connections between ageing and neurodegenerative diseases. It showcased innovative diagnostic and therapeutic strategies for both human and animal prion diseases, as well as related conditions including Alzheimer's and Parkinson's diseases, prion protein-associated cancers, and renal injury. The programme featured 70 invited talks and 21 selected oral presentations, culminating in 7 plenary sessions led by esteemed speakers, including Nobel Laureate Stanley B. Prusiner. This overview summarizes key presentations and highlights significant aspects of the conference, emphasizing the impactful discussions and collaborations that emerged from this historic event.
Chronic wasting disease as a model for human prion therapy.
Bordonaro M
Prion · 2025 Dec · PMID 40411807 · Full text
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are fatal neurodegenerative disorders that result from abnormally folded prion proteins. These disorders can be sporadic, acquired, or genet...
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are fatal neurodegenerative disorders that result from abnormally folded prion proteins. These disorders can be sporadic, acquired, or genetic. Acquired TSEs can be found in a number of animal species including sheep (scrapie), cows (bovine spongiform encephalopathy), and cervids (chronic wasting disease). Chronic wasting disease (CWD) is unusual in that it is found in free ranging animals in their natural environment. There has been heretofore no reported cases of CWD being transmitted to humans; however, the possibility of future adaption for human transmission exists. Several novel approaches for the prevention and treatment of prion disease in humans are under development, including knockdown of endogenous prion expression or overexpression of dominant negative prion forms. Here, I propose that CWD, as a naturally occurring prion disease, should be considered an important testing target for such therapies, which can demonstrate efficacy outside of controlled laboratory environments. Further, from the ethical standpoint of reducing animal suffering, decreasing the CWD burden in cervid populations is highly desirable. Finally, lowering CWD incidence can reduce future possibilities of transmission to humans or to other animal species.
Functional amyloid protein FXR1 is recruited into neuronal stress granules.
Valina AA, Belashova TA, Yuzman AK … +5 more , Zadorsky SP, Sysoev EI, Mitkevich VA, Makarov AA, Galkin AP
Prion · 2025 Dec · PMID 40411539 · Full text
The FXR1 protein regulates the stability and translation of a number of RNA molecules and plays an important role in the regulation of cellular processes under normal conditions and stress. In particular, this protein is...
The FXR1 protein regulates the stability and translation of a number of RNA molecules and plays an important role in the regulation of cellular processes under normal conditions and stress. In particular, this protein is known to be a negative regulator of the key proinflammatory cytokine TNF alpha. We had previously shown that FXR1 functioned in the amyloid form in neurons of the brain of jawed vertebrates. Under stress conditions, FXR1 is incorporated into stress granules in some cell lines, but such studies have not been conducted for neuronal cells. Here, we showed the ability of the FXR1 protein to form cytoplasmic granules in a neuroblastoma cell line under various types of stress. This protein colocalizes with core proteins of neuronal stress granules upon heat shock and sodium arsenite treatment. We also showed that FXR1 colocalizes with anti-amyloid antibodies OC under both normal and stress conditions. Given that stress granules are dynamic structures, we propose that amyloid FXR1-containing RNP particles interact with other stress granule proteins through weak intermolecular hydrogen bonds. Using a yeast model system, we found that FXR1 colocalizes and physically interacts with stress granule proteins such as TIA-1, FMRP, FXR2, and SFPQ. Overall, our results provide new insights into the role of the RNA-binding protein FXR1 in neuronal stress response. We believe that FXR1 inactivation in neuronal stress granules can contribute to an increase in the level of the proinflammatory cytokine TNF alpha in neurodegenerative diseases.
Specific early electroencephalogram for the diagnosis of sporadic Creutzfeldt-Jakob disease.
Matsubayashi T, Natsui H, Satoh K … +3 more , Kitamoto T, Yokota T, Sanjo N
Prion · 2025 Dec · PMID 40125901 · Full text
An early diagnosis is required for intervention in prion disease cases. To elucidate the specificity of early electroencephalography discharges in cases of sporadic Creutzfeldt-Jakob disease, we analysed epileptiform dis...
An early diagnosis is required for intervention in prion disease cases. To elucidate the specificity of early electroencephalography discharges in cases of sporadic Creutzfeldt-Jakob disease, we analysed epileptiform discharges through electroencephalography. Nine patients with methionine/methionine type 1/classic sporadic Creutzfeldt-Jakob disease and 20 patients with status epilepticus were included. Generalized periodic discharges, lateralized periodic discharges, and central sagittal sporadic epileptiform discharges were evaluated. Central sagittal sporadic epileptiform discharges were defined as nonrhythmic and nonperiodic waveforms showing generalized spike-and-wave complexes and/or sharp waves predominantly in the central sagittal region. In the sporadic Creutzfeldt-Jakob disease group, central sagittal sporadic epileptiform discharges, lateralized periodic discharges, and generalized periodic discharges were observed in five (55.6%), one (11.1%), and eight (88.9%) patients, respectively, with an average duration from onset to the appearance of the discharges of 1.6, 1.0, and 2.44 months, respectively. In the status epilepticus group, these discharges were detected in one (5.0%), six (30.0%), and six (30.0%) patients, respectively. The incorporation of central sagittal sporadic epileptiform discharges and lateralized periodic discharges into the World Health Organization diagnostic criteria, alongside generalized periodic discharges, significantly shortened the average lapse from symptom onset to sporadic Creutzfeldt-Jakob disease diagnosis (2.06 months vs. 2.44 months; = 0.02). Central sagittal sporadic epileptiform discharges emerge as promising biomarkers for distinguishing sporadic Creutzfeldt-Jakob disease from status epilepticus, and together with lateralized periodic discharges provide an opportunity for early diagnosis of sporadic Creutzfeldt-Jakob disease.
Chronic Wasting Disease Research in North America: A systematic review highlighting species-wise and interdisciplinary research trends.
Rg C, Tallon A, Latch EK
Prion · 2025 Dec · PMID 39960789 · Full text
Chronic Wasting Disease (CWD) research has experienced significant growth, spanning diverse disciplines such as genetics, immunology, modelling, and behaviour. To gain a broad understanding of the changes in CWD research...
Chronic Wasting Disease (CWD) research has experienced significant growth, spanning diverse disciplines such as genetics, immunology, modelling, and behaviour. To gain a broad understanding of the changes in CWD research focusing cervids, we analysed temporal trends in study location, species, genus investigated, infection types, and population type since the discovery of CWD in 1980s. Our findings indicate that Colorado, USA, published the highest number of articles, followed by Wisconsin, and publication numbers correlated with reported CWD cases in states/provinces. emerged as the most studied genus. Wild populations are studied more commonly than captive populations. Keyword analysis of transmission types shows the discovery of novel transmission modes in the recent past. We also used a novel approach to categorize studies into five themes: field-based, lab-based, math/analytics/modelling-based, management-based, and human dimensions. Overall, most studies captured had a lab-based component. The interdisciplinary or transdisciplinary nature of major disciplines and evolving trends in keywords, particularly the increased reliance on genetics/genomics, accentuate the beginning of using genomics to under and tackle CWD at a fundamental scale. Encapsulated in our analysis, these dynamic changes offer valuable insights for navigating CWD through scientifically informed proactive management decisions in conjunction with existing surveillance efforts not only for the commonly studied species but also for potentially susceptible species.
Genetic assessment of apolipoprotein E polymorphism and PRNP genotypes in rapidly progressive dementias in Pakistan.
Rasheed U, Khalid M, Noor A … +3 more , Saeed U, Uppal R, Zafar S
Prion · 2024 Dec · PMID 39654135 · Full text
Rapidly progressive dementias (RPDs) are a type of fatal dementias that cause rapid progression of neuronal dysfunction. This study aimed to assess the prevalence of APOE genotypes (ε2, ε3, ε4) and PRNP mutations (E200K,...
Rapidly progressive dementias (RPDs) are a type of fatal dementias that cause rapid progression of neuronal dysfunction. This study aimed to assess the prevalence of APOE genotypes (ε2, ε3, ε4) and PRNP mutations (E200K, M129V) in the general population of Pakistan because of their association with RPDs, including Rapidly Progressive Alzheimer's Disease (rpAD) and Creutzfeldt-Jakob Disease (CJD). Blood samples ( = 100) were collected from healthy Pakistani population and the stated mutations were assessed using polymerase chain reaction. In the analysis of the APOE genotype, ε3/ε3 genotype was the most common (95%), followed by ε3/ε4 (5%) and ε2 allele was completely absent. A low frequency of ε4 allele and the absence of a protective ε2 allele is associated with an increased risk of rpAD. In the case of PRNP mutations, the most common genotype was M129-Ε200 (71%) and V129-Ε200 (29%). E200K mutation was completely absent from the given population. It is noteworthy that the MM homozygous genotype was present in 71 samples, VV genotype was present in 29. Homozygosity on codon 129, as observed in most of our samples, has been associated with more efficient production of PrP and disease pathology. This study provides preliminary data indicating that rpAD and CJD pose a significant threat to the Pakistani population.
Expression of the cellular prion protein by mast cells in white-tailed deer carotid body, cervical lymph nodes and ganglia.
Kincaid AE, Denkers ND, McNulty EE … +3 more , Kraft CN, Bartz JC, Mathiason CK
Prion · 2024 Dec · PMID 39285618 · Full text
Chronic wasting disease (CWD) is a transmissible and fatal prion disease that affects cervids. While both oral and nasal routes of exposure to prions cause disease, the spatial and temporal details of how prions enter th...
Chronic wasting disease (CWD) is a transmissible and fatal prion disease that affects cervids. While both oral and nasal routes of exposure to prions cause disease, the spatial and temporal details of how prions enter the central nervous system (CNS) are unknown. Carotid bodies (CBs) are structures that are exposed to blood-borne prions and are densely innervated by nerves that are directly connected to brainstem nuclei, known to be early sites of prion neuroinvasion. All CBs examined contained mast cells expressing the prion protein which is consistent with these cells playing a role in neuroinvasion following prionemia.
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