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> Disorders > Disease or Syndrome > Prion Diseases

Prion Diseases

Prion Diseases are a group of rare, fatal neurodegenerattive disorders caused by misfolded prion proteins.
They affect both humans and animals, and include conditions like Creutzfeldt-Jakob Disease, Bovine Spongiform Encephalopathy (known as 'mad cow disease'), and Chronic Wasting Disease in deer and elk.
Prion Diseases lead to progressive brain damage and are challenging to diagnose and treat.
Understanding the underlying mechanisms and developing effective therapies are critical research priorities in this field.

Most cited protocols related to «Prion Diseases»

1
Comprehensive Prion Disease Pathology Analysis
The study was based on tissue samples from subjects affected by various subtypes of human prion disease, including the whole spectrum of currently characterized human prion strains [30 (link)]. All cases were selected from a larger pool of pathological material based on the following essential criteria: (1) availability of all necessary brain structures (see below); (2) inclusion of all known sporadic TSE subtypes according to the updated classification of Parchi et al. [31 (link)] as well as vCJD; and (3) absence of additional significant pathological comorbidity, such as “intermediate” or “high” Alzheimer’s disease neuropathological changes [19 (link)], cerebral haemorrhages or infarcts, or a known history of neurological disorders other than prion disease. PRNP genetics and PrPSc typing had been performed in all selected cases as described previously [10 (link), 31 (link)]. PrPSc typing, in particular, was performed in each case in at least six brain samples (frontal, temporal, parietal, and occipital cortices, thalamus, and cerebellum). Local ethical committee approval (Medical Ethics Committee of the Ludwig Maximilians University, Munich) was obtained for the study of autopsy material, with written informed consent for research use provided by the patients during life or by their next of kin after death.
A total of 21 cases were included. Two “atypical” CJD cases (i.e. not fitting any of the subtypes defined by the current CJD classification) were also added to the series. The total number and anatomical representation of the sections included in the study were chosen by the reference group (PP, AG, and HK). The two major aims were on the one hand to keep the number of slides to a minimum and on the other to select all brain regions that highlight the distinctive features of each TSE subtype [11 (link), 30 (link), 31 (link)].
All selected cases displayed histopathological lesions and PrP-immunoreactive deposits.
Two sets of 4 μm thick sections were produced. Each set contained haematoxylin and eosin (H&E) stained sections from seven brain areas (frontal and occipital cortices, hippocampus, striatum, thalamus, medulla, and cerebellum) of the 21 cases, as well as sections stained for PrP by immunohistochemistry from the frontal and occipital cortices, hippocampus, and cerebellum of all cases. All sections were stained using the same methodology in one laboratory (LMU, München). Specimens were sent blindly with a combined letter and numerical code together with the operative instructions (see below).
Parchi P., de Boni L., Saverioni D., Cohen M.L., Ferrer I., Gambetti P., Gelpi E., Giaccone G., Hauw J.J., Höftberger R., Ironside J.W., Jansen C., Kovacs G.G., Rozemuller A., Seilhean D., Tagliavini F., Giese A, & Kretzschmar H.A. (2012). Consensus classification of human prion disease histotypes allows reliable identification of molecular subtypes: an inter-rater study among surveillance centres in Europe and USA. Acta neuropathologica, 124(4), 517-529.
Publication 2012
Autopsy Brain Cerebellum Cerebral Hemorrhage Cuneus Eosin Ethics Committees Homo sapiens Immunohistochemistry Infarction Medulla Oblongata Nervous System Disorder New Variant Creutzfeldt-Jakob Disease Patients Prion Diseases Prions Seahorses Strains Striatum, Corpus Thalamus Tissues
2
Recruiting Patients for Prion Disease Trial
To ensure that PRION-1 enrolled a sufficient number of patients, recruitment of a high proportion of all UK patients with prion disease was needed because of the rarity of the diseases. A national referral system was set up to recruit patients while continuing to support ongoing epidemiological studies and surveillance. In 2004, all UK neurologists were asked by the Chief Medical Officer to refer all patients with suspected prion disease jointly to the National CJD Surveillance Unit (Edinburgh, UK) and to the National Prion Clinic (London, UK), enabling participation in research, including the PRION-1 trial. Before the formal launch of PRION-1, patients attending the National Prion Clinic could enter a pilot phase of the trial in which randomisation was not offered. Patients with any form of human prion disease who met standard diagnostic criteria10 and who were aged 12 years or older were eligible. Individuals with known hypersensitivity to quinacrine, who had taken any other potential antiprion drug within the past 2 months, or who clinicians judged to be in a terminal disease state were ineligible. All referred patients or their carers were contacted to ask if they would agree to a home or clinic screening visit from the PRION-1 team. Patients were seen at enrolment and subsequently either at the National Prion Clinic or at their homes by the same members of the PRION-1 clinical team. The PRION-1 trial was approved by the Eastern Multicentre Research Ethics Committee. All patients gave consent, or assent was provided by a family member or independent neurologists.
Collinge J., Gorham M., Hudson F., Kennedy A., Keogh G., Pal S., Rossor M., Rudge P., Siddique D., Spyer M., Thomas D., Walker S., Webb T., Wroe S, & Darbyshire J. (2009). Safety and efficacy of quinacrine in human prion disease (PRION-1 study): a patient-preference trial. The Lancet. Neurology, 8(4), 334-344.
Publication 2009
Clinic Visits Diagnosis Ethics Committees, Research Family Member Homo sapiens Hypersensitivity Neurologists Patients Pharmaceutical Preparations Prion Diseases Prions Quinacrine Rare Diseases Vision
3
Nationwide Prion Disease Cohort Study
From 2004, UK neurologists were asked by the chief medical officer of the Department of Health, England, to refer all patients with suspected prion disease jointly to the National CJD Research and Surveillance Unit and to the National Health Service National Prion Clinic. Communication between both units several times per week ensures exchange of patient details referred to one of the units. Eighty-five percent of patients were visited by the National Prion Clinic within 5 days of referral. Details of enrollment into the PRION-1 Trial and cohort study have been published.10 (link),13 (link) In brief, the cohort aimed to enroll all symptomatic patients with prion disease in the United Kingdom including all patients with probable or definite sCJD, variant CJD, iatrogenic CJD, and inherited prion disease, according to updated diagnostic criteria.17 (link) In addition, patients thought to have prion disease but not meeting formal criteria could be enrolled following review by an expert panel. Patients were enrolled at home, hospitals, and other health care settings around the United Kingdom from 2008 onwards (Figure 1). This current study was conducted from October 2008 to June 2014.
Mead S., Burnell M., Lowe J., Thompson A., Lukic A., Porter M.C., Carswell C., Kaski D., Kenny J., Mok T.H., Bjurstrom N., Franko E., Gorham M., Druyeh R., Wadsworth J.D., Jaunmuktane Z., Brandner S., Hyare H., Rudge P., Walker A.S, & Collinge J. (2016). Clinical Trial Simulations Based on Genetic Stratification and the Natural History of a Functional Outcome Measure in Creutzfeldt-Jakob Disease. JAMA neurology, 73(4), 447-455.
Publication 2016
Creutzfeldt-Jakob Disease, Sporadic Diagnosis Health Services, National Hereditary Diseases Neurologists Patients Prion Diseases Prions
4
Estimating Disease Risk from Genotypes
By Bayes' theorem, the probability of disease given a genotype
(penetrance or lifetime risk, P(D|G)) is equal to the proportion of individuals
with the disease who have the genotype (genotype frequency in cases, P(G|D))
times the prevalence of the disease (baseline lifetime risk in the general
population, P(D)), divided by the frequency of the genotype in the general
population (here, population control allele frequency, P(G)). The use of this
formula to estimate disease risk dates back at least to Cornfield's
estimation of the probability of lung cancer in smokers (107 (link)), with later contributions by Woolf (108 (link)) and a synthesis by C.C. Li with
application to genetics (109 ).
We used an allelic rather than genotypic model, such that lifetime risk
in an individual with one allele is equal to case allele frequency (based on the
number of prion disease cases that underwent PRNP sequencing)
times baseline risk divided by population control allele frequency, P(D|A) =
P(A|D)×P(D)/P(A). Note that we assume that our population control
datasets include individuals who will later die of prion disease, thus enabling
direct use of the ExAC and 23andMe allele frequencies as the denominator P(A).
Following Kirov (11 (link)), we compute Wilson
95% confidence intervals on the binomial proportions P(A|D) and P(A),
and calculate the upper bound of the 95% confidence interval for
penetrance using the upper bound on case allele frequency and the lower bound on
population control allele frequency, and vice versa for the lower bound on
penetrance.
Minikel E.V., Vallabh S.M., Lek M., Estrada K., Samocha K.E., Sathirapongsasuti J.F., McLean C.Y., Tung J.Y., Yu L.P., Gambetti P., Blevins J., Zhang S., Cohen Y., Chen W., Yamada M., Hamaguchi T., Sanjo N., Mizusawa H., Nakamura Y., Kitamoto T., Collins S.J., Boyd A., Will R.G., Knight R., Ponto C., Zerr I., Kraus T.F., Eigenbrod S., Giese A., Calero M., de Pedro-Cuesta J., Haïk S., Laplanche J.L., Bouaziz-Amar E., Brandel J.P., Capellari S., Parchi P., Poleggi A., Ladogana A., O'Donnell-Luria A.H., Karczewski K.J., Marshall J.L., Boehnke M., Laakso M., Mohlke K.L., Kähler A., Chambert K., McCarroll S., Sullivan P.F., Hultman C.M., Purcell S.M., Sklar P., van der Lee S.J., Rozemuller A., Jansen C., Hofman A., Kraaij R., van Rooij J.G., Ikram M.A., Uitterlinden A.G., van Duijn C.M., Daly M.J, & MacArthur D.G. (2016). Quantifying penetrance in a dominant disease gene using large population control cohorts. Science translational medicine, 8(322), 322ra9.
Publication 2016
Alleles Anabolism Genotype Lung Cancer Prion Diseases
5
Prion Disease Diagnostic Workflow
The specimens of blood, CSF and brain tissues of the suspected patient were collected by the sentinel hospital. All samples were transported to the national reference laboratory for human prion disease in CCDC. The peripheral blood leukocytes were used for sequencing analysis of PRNP and polymorphism of codon 129, with an automatic genetic analyzer (ABI3130XL). CSF samples were obtained by routine lumbar puncture and analysed by Western immunoblot to detect the 14-3-3 protein. Brain tissues obtained from autopsy or biopsy were applied into neuropathologic assays and/or PrPSc detections with immunohistochemistry and/or Western blot. The standard operation procedure (SOP) of each test was well documented in the CJD surveillance program, which was described previously [4] .
Gao C., Shi Q., Tian C., Chen C., Han J., Zhou W., Zhang B.Y., Jiang H.Y., Zhang J, & Dong X.P. (2011). The Epidemiological, Clinical, and Laboratory Features of Sporadic Creutzfeldt-Jakob Disease Patients in China: Surveillance Data from 2006 to 2010. PLoS ONE, 6(8), e24231.
Publication 2011
14-3-3 Proteins Autopsy Biological Assay Biopsy BLOOD Brain Codon Genetic Polymorphism Homo sapiens Immunohistochemistry Leukocytes Patients Prion Diseases Punctures, Lumbar Sequence Analysis Tissues Western Blot Western Blotting

Most recents protocols related to «Prion Diseases»

1
Resilience to Severe Alzheimer's Pathology

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Open the protocol to access the free full text link

Publication 2023
Amyotrophic Lateral Sclerosis Ataxia, Spinocerebellar Autopsy Cognition Demyelinating Diseases Diagnosis Disorders, Cognitive Frontotemporal Lobar Degeneration Huntington Disease Leukoencephalopathy Malformations of Cortical Development Multiple Sclerosis Neoplasms Patients Prion Diseases Respiratory Diaphragm Trinucleotide Repeats
2
Prion Disease Onset Delay Assessed
All studies were conducted at the McLaughlin Research Institute between June 2014 and June 2016 under IACUC approval MRI-GAC11. In addition to the mouse orthologs of the D178N and E200K mutations, the ki-3F4-FFI and ki-3F4-CJD alleles also contain the 3F4 epitope common to many mammals other than mice, which allows detection with the 3F4 antibody. To control for any impact that this might have on disease outcomes, we used ki-3F4-WT mice, which also have this epitope but no mutation and do not develop spontaneous disease (8 (link)), as a control group. Under the expectation that the onset of astrocytosis would occur at the age of 13 ± 3 months (mean ± SD), a sample size of 10 per group was calculated to provide 80% power (by a 2-sided t test) to detect a 30% delay in onset; anle138b in RML prion-infected mice had been reported to delay disease by 30 to 97% depending on the time point of treatment initiation (6 (link)). Because mice would be subject to humane euthanasia, we also included survival as an endpoint. Finally, we included histopathology because spongiform changes and PrP deposition are pathognomonic for prion disease. Animal care and histology scoring were performed in an unblind manner.
Vallabh S.M., Zou D., Pitstick R., O’Moore J., Peters J., Silvius D., Kriz J., Jackson W.S., Carlson G.A., Minikel E.V, & Cabin D.E. (2023). Therapeutic Trial of anle138b in Mouse Models of Genetic Prion Disease. Journal of Virology, 97(2), e01672-22.
Publication 2023
3-(1,3-benzodioxol-5-yl)-5-(3-bromophenyl)-1H-pyrazole Alleles Animals Astrocytosis Epitopes Euthanasia Immunoglobulins Institutional Animal Care and Use Committees Mammals Mice, Laboratory Mutation Porifera Prion Diseases Prions
3
Prion Disease Animal Ethics Protocol
All work with animals was performed in compliance with the Canadian Council on Animal Care Guidelines and Policies. All procedures involving animals were reviewed and approved by the Health Sciences Animal Care and Use Committee of the University of Alberta under protocol “Etiology and Pathogenesis of Prion Diseases” AUP # 914.
Kuznetsova A., McKenzie D., Ytrehus B., Utaaker K.S, & Aiken J.M. (2023). Movement of Chronic Wasting Disease Prions in Prairie, Boreal and Alpine Soils. Pathogens, 12(2), 269.
Publication 2023
Animals pathogenesis Prion Diseases
4
Determining TSE Status from RT-QuIC Data
To identify the methods used by researchers to determine TSE status from RT-QuIC data, we conducted a PubMed search (keywords: RT-QuIC and “real-time quaking-induced conversion”) for articles that performed RT-QuIC between 2012 and 2021. Studies were selected if the researchers both performed RT-QuIC and implemented a rubric for determining TSE status. Studies were not vetted for any particular prion disease or proteopathy.
Rowden G.R., Picasso-Risso C., Li M., Schwabenlander M.D., Wolf T.M, & Larsen P.A. (2023). Standardization of Data Analysis for RT-QuIC-Based Detection of Chronic Wasting Disease. Pathogens, 12(2), 309.
Publication 2023
Prion Diseases
5
Tg66 Transgenic Mice for Prion Disease
Tg66 transgenic mice overexpressing human PrPC were used for this study. These mice have been shown to be susceptible to prion disease by infection with MV1 and 2 sCJD prions, with distinct disease courses and biochemistry apparent with the different inocula [23 (link)]. Generation of these mice was described previously [22 (link)]. Tg66 mice were originally made by Richard Rubenstein and provided to RML by Robert Rohwer. Tg66 mice are on an FVB/N genetic background and are homozygous for a transgene that encodes human prion protein M129. Tg66 mice overexpress human PrPC at 8–16-fold levels higher than normal physiologic levels and have been shown to be susceptible to vCJD, sCJD and mouse-adapted 22L scrapie [22 (link), 24 (link)]. Tg66 mice do not express any normal mouse PrPC.
Groveman B.R., Race B., Foliaki S.T., Williams K., Hughson A.G., Baune C., Zanusso G, & Haigh C.L. (2023). Sporadic Creutzfeldt–Jakob disease infected human cerebral organoids retain the original human brain subtype features following transmission to humanized transgenic mice. Acta Neuropathologica Communications, 11, 28.
Publication 2023
Creutzfeldt-Jakob Disease, Sporadic Disease Progression Genetic Background Homo sapiens Homozygote Infection Mice, Laboratory Mice, Transgenic New Variant Creutzfeldt-Jakob Disease NR4A2 protein, human physiology Prion Diseases Prions Scrapie Transgenes

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1
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2
Biocare mouse on mouse horseradish peroxidase polymer by Biocare Medical
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3
Tesee by Bio-Rad
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The TeSeE is a compact and automated instrument for the detection and quantification of prion proteins. It is designed to perform rapid and reliable analysis of biological samples, providing accurate and consistent results.
4
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More about "Prion Diseases"

Prion diseases are a group of rare, fatal neurodegenerative conditions characterized by the misfolding of prion proteins.
These disorders affect both humans and animals, including Creutzfeldt-Jakob Disease (CJD), Bovine Spongiform Encephalopathy (BSE, also known as 'mad cow disease'), and Chronic Wasting Disease (CWD) in deer and elk.
These prion disorders lead to progressive brain damage and are challenging to diagnose and treat effectively.
Understanding the underlying mechanisms and developing effective therapies are critical research priorities in this field.
Techniques like the Omni Tissue Homogenizer, Biocare Mouse on Mouse Horseradish Peroxidase Polymer, and the TeSeE assay can be used to analyze and study prion diseases.
Animal models like C57BL/6 mice are commonly used in prion research, often with the support of cell culture media like Fetal Bovine Serum (FBS).
Labeling techniques such as BrdU can help track cellular processes, while tools like the BeadBlaster 24 and INNOTEST platforms can assist in sample preparation and analysis.
Leveraging the power of AI-driven platforms like PubCompare.ai can enhance research reproducibility for prion diseases.
These tools enable researchers to easily locate the best protocols from literature, preprints, and patents, using intelligent comparisons to identify the most reliable and effective methods for their work.
Improving the quality and consistency of findings in prion disease research is crucial, as these conditions remain challenging to diagnose and treat effectively.