Assessing Prion Infectivity of Human Urine in Sporadic Creutzfeldt-Jakob Disease

Notari, Silvio; Qing, Liuting; Pocchiari, Maurizio; Dagdanova, Ayuna; Hatcher, Kristin Ward; Dogterom, Arend; Groisman, Jose F.; Lumholtz, I. B.; Puopolo, Maria; Lasmézas, Corinne Ida; Chen, Shu G.; Kong, Qingzhong

doi:10.3201/eid1801.110589

Cited by 21 publications

(18 citation statements)

References 39 publications

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“…Further details on quantitative mass spectrometry relating to comparative analyses can be obtained from [76]. Other protocols can be used to focus on spectral counting quantification specifically [77], with relevance to extracellular vesicles [16][17][18]78]. 9.…”

Section: Notesmentioning

confidence: 99%

“…Detection of infectious prions has been validated in several biological fluids including urine, saliva, milk, and blood of infected animals through different experimental strategies like in vivo bioassays, protein misfolding cyclic amplification (PMCA), or by realtime quaking-induced conversion (RT-QuIC; [72][73][74][75][76][77][78][79][80][81][82][83][84][85][86][87][88]). In this respect, recent studies revealed the association of pathological PrP with exosomes released in blood of infected animals [89,90].…”

Section: Introductionmentioning

confidence: 99%

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Exosomes and Microvesicles

Hill¹

2017

Methods in Molecular Biology

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Section: Notesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Exosomes and Microvesicles

Hill¹

2017

Methods in Molecular Biology

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“…-The amount of prion infectivity that is below the threshold of detectability of a mouse bioassay but that might be present in the studied tissue can be estimated in infectious units (IU) per millilitre with 95 % CI (rather than in 50 % infectious dose (ID 50 )) by assuming a Poisson distribution in the response variable, as proposed by Notari et al (2012).…”

Section: Overall Considerationsmentioning

confidence: 99%

Protocol for further laboratory investigations into the distribution of infectivity of Atypical BSE

2014

EFSA Journal

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Information on the pathogenesis and tissue distribution of Atypical Bovine Spongiform Encephalopathy (BSE) in cattle through the study of field cases and experimental transmission studies is lacking. The latter are limited to transmission of Atypical BSE through intracerebral (i.c.) inoculation of cattle. All data currently available relate to the presence or absence of PrP Sc , but do not quantify relative amounts of PrP Sc or levels of infectivity. A laboratory protocol for further studies is recommended, to allow the assessment of the relative infectious titre, PrP Sc accumulation and prion seeding activity in the tissues of cattle that developed H-BSE or L-BSE (using posterior brainstem as a reference). Tissues to be covered by those studies are categorised in three priorities, based on their inclusion in the list of specific risk material in cattle, on the presence of infectivity, or PrP Sc presence, demonstrated in Atypical BSEs or other Transmissible Spongiform Encephalopathies (TSEs) in ruminants, and on the importance in terms of input into the food chain in the EU. The protocol provides details in terms of the minimum number of animals to be tested, processing and preparation of tissues, and methods to be used to identify abnormal PrP and quantify infectivity, also depending on the expected level of infectivity and amount of tissue available for analysis. It is recommended that, through the implementation of the protocol, information should also be obtained on the performance of currently validated rapid tests for TSE active surveillance in cattle/bioassay for detecting H-BSE and L-BSE agents.

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“…The same peptides can be detected by new electrochemical detection immuno-sensors. These biosensors are based on immobilization of antibodies on gold nanostructured Identification of phosphorylated biomarkers pTau181, pTau199 and pTau231 in CSF by immunoassays [162][163][164][165][166][167] Cerebral amyloid angiopathy Aβ peptide Early phase PET imaging of cerebral fibrillary β-amyloid with 11C-Pittsburgh compound B as a PET ligand [168][169][170] PD α-Syn Detection of α-Syn aggregates in biotic samples by imunohistochemical or fluorescent staining [171][172][173] Multi-parametric fluorescent pyrene-labelling of biotic samples [174] Detection of α-Syn oligomers in human plasma or red cells by ELISA [175,176] Huntington's Disease Htt Loss of brain volume observed by MRI with combination of genetic test -identification of abnormal CAG expansion in exon1 of htt gene [177][178][179] Variant Creutzfeldt-Jakob disease Prion protein PrP Whole blood immunoassay [180][181][182] Other prion diseases: Gerstmann-Sträussler-Scheinker disease, fatal familial insomnia, kuru, Creutzfeldt-Jakob Disease Prion protein PrP Conformation dependent immunoassays in biopsy samples [183,184] Analysis of 14-3-3 and PrPSc expression pattern in CSF [185] Detection of PrPSc in urine by immunoassay [186,187] screen-printed electrodes with cyclic voltammetry detection [115], or with difference pulse voltammetry detection with immobilization on gelsolin coated electrodes that selectively binds Aβ peptides [116]. Another interesting approach combines ELISA and surface plasmon resonance to provide greatly enhanced detection, using gold nano-particles conjugated with antibodies [117].…”

Section: Clinical Detection Of Protein Aggregatesmentioning

confidence: 99%

Detection of mis-folded protein aggregates from a clinical perspective

et al. 2016

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Neurodegenerative Protein Misfolding Diseases (PMDs), such as Alzheimer's (AD), Parkinson's (PD) and prion diseases, are generally difficult to diagnose before irreversible damage to the central nervous system damage has occurred. Detection of the misfolded proteins that ultimately lead to these conditions offers a means for providing early detection and diagnosis of this class of disease. In this review, we discuss recent developments surrounding protein misfolding diseases with emphasis on the cytotoxic oligomers implicated in their aetiology. We also discuss the relationship of misfolded proteins with biological membranes. Finally, we discuss how far techniques for providing early diagnoses for PMDs have advanced and describe promising clinical approaches. We conclude that antibodies with specificity towards oligomeric species of AD and PD and lectins with specificity for particular glycosylation, show promise. However, it is not clear which approach may yield a reliable clinical test first. Relevance for patients: Individuals suffering from protein misfolding diseases will likely benefit form earlier, less-or even non-invasive diagnosis techniques. The current state and possible future directions for these are subject of this review.

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Assessing Prion Infectivity of Human Urine in Sporadic Creutzfeldt-Jakob Disease

Abstract: Intracerebral inoculation of transgenic mice failed to demonstrate prion disease transmission.

Cited by 21 publications

References 39 publications

Exosomes and Microvesicles

Exosomes and Microvesicles

Protocol for further laboratory investigations into the distribution of infectivity of Atypical BSE

Detection of mis-folded protein aggregates from a clinical perspective

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