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  1. Book: Prion diseases

    Collinge, John

    1997  

    Author's details ed. by John Collinge
    Keywords Prion Diseases ; Prion ; Infektionskrankheit
    Subject Ansteckende Krankheit ; Kontagiöse Krankheit ; Infektionskrankheiten
    Language English
    Size 205 S. : Ill., graph. Darst.
    Publisher Oxford Univ. Press
    Publishing place Oxford u.a.
    Publishing country Great Britain
    Document type Book
    HBZ-ID HT007460386
    ISBN 0-19-854789-7 ; 978-0-19-854789-1
    Database Catalogue ZB MED Medicine, Health

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  2. Article ; Online: Mammalian prions and their wider relevance in neurodegenerative diseases.

    Collinge, John

    Nature

    2016  Volume 539, Issue 7628, Page(s) 217–226

    Abstract: Prions are notorious protein-only infectious agents that cause invariably fatal brain diseases following silent incubation periods that can span a lifetime. These diseases can arise spontaneously, through infection or be inherited. Remarkably, prions are ...

    Abstract Prions are notorious protein-only infectious agents that cause invariably fatal brain diseases following silent incubation periods that can span a lifetime. These diseases can arise spontaneously, through infection or be inherited. Remarkably, prions are composed of self-propagating assemblies of a misfolded cellular protein that encode information, generate neurotoxicity and evolve and adapt in vivo. Although parallels have been drawn with Alzheimer's disease and other neurodegenerative conditions involving the deposition of assemblies of misfolded proteins in the brain, insights are now being provided into the usefulness and limitations of prion analogies and their aetiological and therapeutic relevance.
    MeSH term(s) Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/classification ; Amyloid beta-Peptides/metabolism ; Animals ; Humans ; Kinetics ; Mammals ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neurodegenerative Diseases/therapy ; Prions/chemistry ; Prions/genetics ; Prions/metabolism ; Prions/toxicity ; Protein Folding
    Chemical Substances Amyloid beta-Peptides ; Prions
    Language English
    Publishing date 2016-11-10
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/nature20415
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  3. Article ; Online: Prion strains viewed through the lens of cryo-EM.

    Manka, Szymon W / Wenborn, Adam / Collinge, John / Wadsworth, Jonathan D F

    Cell and tissue research

    2022  Volume 392, Issue 1, Page(s) 167–178

    Abstract: Mammalian prions are lethal transmissible pathogens that cause fatal neurodegenerative diseases in humans and animals. They consist of fibrils of misfolded, host-encoded prion protein (PrP) which propagate through templated protein polymerisation. Prion ... ...

    Abstract Mammalian prions are lethal transmissible pathogens that cause fatal neurodegenerative diseases in humans and animals. They consist of fibrils of misfolded, host-encoded prion protein (PrP) which propagate through templated protein polymerisation. Prion strains produce distinct clinicopathological phenotypes in the same host and appear to be encoded by distinct misfolded PrP conformations and assembly states. Despite fundamental advances in our understanding of prion biology, key knowledge gaps remain. These include precise delineation of prion replication mechanisms, detailed explanation of the molecular basis of prion strains and inter-species transmission barriers, and the structural definition of neurotoxic PrP species. Central to addressing these questions is the determination of prion structure. While high-resolution definition of ex vivo prion fibrils once seemed unlikely, recent advances in cryo-electron microscopy (cryo-EM) and computational methods for 3D reconstruction of amyloids have now made this possible. Recently, near-atomic resolution structures of highly infectious, ex vivo prion fibrils from hamster 263K and mouse RML prion strains were reported. The fibrils have a comparable parallel in-register intermolecular β-sheet (PIRIBS) architecture that now provides a structural foundation for understanding prion strain diversity in mammals. Here, we review these new findings and discuss directions for future research.
    MeSH term(s) Cricetinae ; Humans ; Mice ; Animals ; Prions/metabolism ; Cryoelectron Microscopy ; Prion Proteins ; Neurodegenerative Diseases ; Mammals/metabolism ; Prion Diseases/metabolism
    Chemical Substances Prions ; Prion Proteins
    Language English
    Publishing date 2022-08-27
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 125067-x
    ISSN 1432-0878 ; 0302-766X
    ISSN (online) 1432-0878
    ISSN 0302-766X
    DOI 10.1007/s00441-022-03676-z
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  4. Article ; Online: Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics.

    Sun, Yuanzi / Jack, Kezia / Ercolani, Tiziana / Sangar, Daljit / Hosszu, Laszlo / Collinge, John / Bieschke, Jan

    ACS nano

    2023  Volume 17, Issue 7, Page(s) 6575–6588

    Abstract: In prion diseases, fibrillar assemblies of misfolded prion protein (PrP) self-propagate by incorporating PrP monomers. These assemblies can evolve to adapt to changing environments and hosts, but the mechanism of prion evolution is poorly understood. We ... ...

    Abstract In prion diseases, fibrillar assemblies of misfolded prion protein (PrP) self-propagate by incorporating PrP monomers. These assemblies can evolve to adapt to changing environments and hosts, but the mechanism of prion evolution is poorly understood. We show that PrP fibrils exist as a population of competing conformers, which are selectively amplified under different conditions and can "mutate" during elongation. Prion replication therefore possesses the steps necessary for molecular evolution analogous to the quasispecies concept of genetic organisms. We monitored structure and growth of single PrP fibrils by total internal reflection and transient amyloid binding super-resolution microscopy and detected at least two main fibril populations, which emerged from seemingly homogeneous PrP seeds. All PrP fibrils elongated in a preferred direction by an intermittent "stop-and-go" mechanism, but each population possessed distinct elongation mechanisms that incorporated either unfolded or partially folded monomers. Elongation of RML and ME7 prion rods likewise exhibited distinct kinetic features. The discovery of polymorphic fibril populations growing in competition, which were previously hidden in ensemble measurements, suggests that prions and other amyloid replicating by prion-like mechanisms may represent quasispecies of structural isomorphs that can evolve to adapt to new hosts and conceivably could evade therapeutic intervention.
    MeSH term(s) Prion Proteins/genetics ; Prion Proteins/metabolism ; Kinetics ; Prions/chemistry ; Amyloid/chemistry ; Amyloidogenic Proteins
    Chemical Substances Prion Proteins ; Prions ; Amyloid ; Amyloidogenic Proteins
    Language English
    Publishing date 2023-02-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1936-086X
    ISSN (online) 1936-086X
    DOI 10.1021/acsnano.2c12009
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  5. Article ; Online: Cell biology. The risk of prion zoonoses.

    Collinge, John

    Science (New York, N.Y.)

    2012  Volume 335, Issue 6067, Page(s) 411–413

    MeSH term(s) Animals ; Brain Chemistry ; Humans ; PrPSc Proteins ; Prion Diseases/transmission ; Spleen/chemistry
    Chemical Substances PrPSc Proteins
    Language English
    Publishing date 2012-01-26
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.1218167
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  6. Article ; Online: Structural differences in amyloid-β fibrils from brains of nondemented elderly individuals and Alzheimer's disease patients.

    Ghosh, Ujjayini / Yau, Wai-Ming / Collinge, John / Tycko, Robert

    Proceedings of the National Academy of Sciences of the United States of America

    2021  Volume 118, Issue 45

    Abstract: Although amyloid plaques composed of fibrillar amyloid-β (Aβ) assemblies are a diagnostic hallmark of Alzheimer's disease (AD), quantities of amyloid similar to those in AD patients are observed in brain tissue of some nondemented elderly individuals. ... ...

    Abstract Although amyloid plaques composed of fibrillar amyloid-β (Aβ) assemblies are a diagnostic hallmark of Alzheimer's disease (AD), quantities of amyloid similar to those in AD patients are observed in brain tissue of some nondemented elderly individuals. The relationship between amyloid deposition and neurodegeneration in AD has, therefore, been unclear. Here, we use solid-state NMR to investigate whether molecular structures of Aβ fibrils from brain tissue of nondemented elderly individuals with high amyloid loads differ from structures of Aβ fibrils from AD tissue. Two-dimensional solid-state NMR spectra of isotopically labeled Aβ fibrils, prepared by seeded growth from frontal lobe tissue extracts, are similar in the two cases but with statistically significant differences in intensity distributions of cross-peak signals. Differences in solid-state NMR data are greater for 42-residue amyloid-β (Aβ42) fibrils than for 40-residue amyloid-β (Aβ40) fibrils. These data suggest that similar sets of fibril polymorphs develop in nondemented elderly individuals and AD patients but with different relative populations on average.
    MeSH term(s) Aged, 80 and over ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/chemistry ; Case-Control Studies ; Female ; Frontal Lobe/pathology ; Humans ; Magnetic Resonance Spectroscopy ; Male ; Plaque, Amyloid/chemistry ; Plaque, Amyloid/pathology
    Chemical Substances Amyloid beta-Peptides
    Language English
    Publishing date 2021-11-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2111863118
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  7. Article ; Online: Overexpression of mouse prion protein in transgenic mice causes a non-transmissible spongiform encephalopathy.

    Jackson, Graham S / Linehan, Jacqueline / Brandner, Sebastian / Asante, Emmanuel A / Wadsworth, Jonathan D F / Collinge, John

    Scientific reports

    2022  Volume 12, Issue 1, Page(s) 17198

    Abstract: Transgenic mice over-expressing human PRNP or murine Prnp transgenes on a mouse prion protein knockout background have made key contributions to the understanding of human prion diseases and have provided the basis for many of the fundamental advances in ...

    Abstract Transgenic mice over-expressing human PRNP or murine Prnp transgenes on a mouse prion protein knockout background have made key contributions to the understanding of human prion diseases and have provided the basis for many of the fundamental advances in prion biology, including the first report of synthetic mammalian prions. In this regard, the prion paradigm is increasingly guiding the exploration of seeded protein misfolding in the pathogenesis of other neurodegenerative diseases. Here we report that a well-established and widely used line of such mice (Tg20 or tga20), which overexpress wild-type mouse prion protein, exhibit spontaneous aggregation and accumulation of misfolded prion protein in a strongly age-dependent manner, which is accompanied by focal spongiosis and occasional neuronal loss. In some cases a clinical syndrome developed with phenotypic features that closely resemble those seen in prion disease. However, passage of brain homogenate from affected, aged mice failed to transmit this syndrome when inoculated intracerebrally into further recipient animals. We conclude that overexpression of the wild-type mouse prion protein can cause an age-dependent protein misfolding disorder or proteinopathy that is not associated with the production of an infectious agent but can produce a phenotype closely similar to authentic prion disease.
    MeSH term(s) Animals ; Brain Diseases/complications ; Humans ; Mammals/metabolism ; Mice ; Mice, Transgenic ; Prion Diseases/metabolism ; Prion Proteins/genetics ; Prions/metabolism
    Chemical Substances Prion Proteins ; Prions
    Language English
    Publishing date 2022-10-13
    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/s41598-022-21608-3
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  8. Article ; Online: Prion protein gene mutation detection using long-read Nanopore sequencing.

    Kroll, François / Dimitriadis, Athanasios / Campbell, Tracy / Darwent, Lee / Collinge, John / Mead, Simon / Vire, Emmanuelle

    Scientific reports

    2022  Volume 12, Issue 1, Page(s) 8284

    Abstract: Prion diseases are fatal neurodegenerative conditions that affect humans and animals. Rapid and accurate sequencing of the prion gene PRNP is paramount to human prion disease diagnosis and for animal surveillance programmes. Current methods for PRNP ... ...

    Abstract Prion diseases are fatal neurodegenerative conditions that affect humans and animals. Rapid and accurate sequencing of the prion gene PRNP is paramount to human prion disease diagnosis and for animal surveillance programmes. Current methods for PRNP genotyping involve sequencing of small fragments within the protein-coding region. The contribution of variants in the non-coding regions of PRNP including large structural changes is poorly understood. Here, we used long-range PCR and Nanopore sequencing to sequence the full length of PRNP, including its regulatory region, in 25 samples from blood and brain of individuals with inherited or sporadic prion diseases. Nanopore sequencing detected the same variants as identified by Sanger sequencing, including repeat expansions/deletions. Nanopore identified additional single-nucleotide variants in the non-coding regions of PRNP, but no novel structural variants were discovered. Finally, we explored somatic mosaicism of PRNP's octapeptide repeat region, which is a hypothetical cause of sporadic prion disease. While we found changes consistent with somatic mutations, we demonstrate that they may have been generated by the PCR. Our study illustrates the accuracy of Nanopore sequencing for rapid and field prion disease diagnosis and highlights the need for single-molecule sequencing methods for the detection of somatic mutations.
    MeSH term(s) Animals ; Mutation ; Nanopore Sequencing ; Prion Diseases/diagnosis ; Prion Diseases/genetics ; Prion Proteins/genetics ; Prion Proteins/metabolism ; Prions/genetics
    Chemical Substances Prion Proteins ; Prions
    Language English
    Publishing date 2022-05-18
    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/s41598-022-12130-7
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  9. Article ; Online: Prevalence and Treatments of Movement Disorders in Prion Diseases: A Longitudinal Cohort Study.

    Sequeira, Danielle / Nihat, Akin / Mok, Tzehow / Coysh, Thomas / Rudge, Peter / Collinge, John / Mead, Simon

    Movement disorders : official journal of the Movement Disorder Society

    2022  Volume 37, Issue 9, Page(s) 1893–1903

    Abstract: Background: Prion diseases cause a range of movement disorders involving the cortical, extrapyramidal, and cerebellar systems, and yet there are no large systematic studies of their prevalence, features, associations, and responses to commonly used ... ...

    Abstract Background: Prion diseases cause a range of movement disorders involving the cortical, extrapyramidal, and cerebellar systems, and yet there are no large systematic studies of their prevalence, features, associations, and responses to commonly used treatments.
    Objectives: We sought to describe the natural history and pharmacological management of movement disorders in prion diseases.
    Methods: We studied the serial examination findings, investigation results, and symptomatic treatment recorded for 700 patients with prion diseases and 51 mimics who had been enrolled onto the prospective longitudinal National Prion Monitoring Cohort study between 2008 and 2020. We performed an analysis to identify whether there were patterns of movement disorders associated with disease aetiology, PRNP codon 129 polymorphism, disease severity rating scales, magnetic resonance imaging (MRI) and cerebrospinal fluid (CSF) findings.
    Results: Gait disturbances, myoclonus, and increased tone are the most frequently observed movement disorders in patients with prion diseases. The typical pattern of early motor dysfunction involves gait disturbance, limb ataxia, impaired smooth pursuit, myoclonus, tremor, and increased limb tone. Disturbances of gait, increased tone, and myoclonus become more prevalent and severe as the disease progresses. Chorea, alien limb phenomenon, and nystagmus were the least frequently observed movement disorders, with these symptoms showing spontaneous resolution in approximately half of symptomatic patients. Disease severity and PRNP codon 129 polymorphism were associated with different movement disorder phenotypes. Antiepileptics and benzodiazepines were found to be effective in treating myoclonus.
    Conclusions: We describe the prevalence, severity, evolution, treatment, and associated features of movement disorders in prion diseases based on a prospective cohort study. © 2022 The Authors. Movement Disorders published by Wiley Periodicals LLC on behalf of International Parkinson and Movement Disorder Society.
    MeSH term(s) Codon ; Cohort Studies ; Creutzfeldt-Jakob Syndrome/genetics ; Creutzfeldt-Jakob Syndrome/pathology ; Humans ; Longitudinal Studies ; Movement Disorders/etiology ; Movement Disorders/genetics ; Myoclonus/genetics ; Prevalence ; Prion Diseases/cerebrospinal fluid ; Prion Diseases/epidemiology ; Prion Diseases/genetics ; Prospective Studies
    Chemical Substances Codon
    Language English
    Publishing date 2022-07-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 607633-6
    ISSN 1531-8257 ; 0885-3185
    ISSN (online) 1531-8257
    ISSN 0885-3185
    DOI 10.1002/mds.29152
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  10. Article ; Online: Estimation of the number of inherited prion disease mutation carriers in the UK.

    Corbie, Rosie / Campbell, Tracy / Darwent, Lee / Rudge, Peter / Collinge, John / Mead, Simon

    European journal of human genetics : EJHG

    2022  Volume 30, Issue 10, Page(s) 1167–1170

    Abstract: Inherited prion diseases (IPD) are a set of rare neurodegenerative diseases that are always caused by mutation of the prion protein gene (PRNP). These are highly heterogeneous in clinical presentation and best described by the specific gene mutation, but ...

    Abstract Inherited prion diseases (IPD) are a set of rare neurodegenerative diseases that are always caused by mutation of the prion protein gene (PRNP). These are highly heterogeneous in clinical presentation and best described by the specific gene mutation, but traditionally include the canonical syndromes familial Creutzfeldt-Jakob disease, Gerstamann-Straussler-Scheinker syndrome, and fatal familial insomnia. In the UK, care of IPD patients and clinical PRNP sequencing have been carried out almost exclusively by the National Prion Clinic and affiliated laboratories since the disease gene was discovered in 1989. Using data obtained over 30 years (1990-2019), this study aimed to provide a greater understanding of the genetic prevalence of IPD using multiple complementary methods. A key source of bias in rare disorders is ascertainment, so we included an analysis based on capture-recapture techniques that may help to minimise ascertainment bias. 225 patients, with 21 different IPD mutations were identified, varying in frequency (with 8/21 mutations comprising over 90% observed cases), derived from 116 kindreds and 151 3-generation families. We estimated a total of 303 UK families (95% CI = 222, 384) segregate IPD mutations, 1091 (95% CI = 720, 1461) UK mutation carriers and a lifetime risk of approximately 1 in 60,000. Simpler methods of measuring prevalence based on extrapolation from the annual incidence of disease, and large scale genomic studies, result in similar estimates of prevalence. These estimates may be of value for planning preventive trials of therapeutics in IPD mutation carriers, prevention of prion disease transmission and provision of specialist services.
    MeSH term(s) Creutzfeldt-Jakob Syndrome/genetics ; Humans ; Mutation ; Prion Diseases/epidemiology ; Prion Diseases/genetics ; Prion Proteins/genetics ; Prion Proteins/metabolism ; Prions/genetics ; United Kingdom/epidemiology
    Chemical Substances Prion Proteins ; Prions
    Language English
    Publishing date 2022-06-27
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1141470-4
    ISSN 1476-5438 ; 1018-4813
    ISSN (online) 1476-5438
    ISSN 1018-4813
    DOI 10.1038/s41431-022-01132-8
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