Detection of prion infection in variant Creutzfeldt-Jakob disease: a blood-based assay

@article{Edgeworth2011DetectionOP,
  title={Detection of prion infection in variant Creutzfeldt-Jakob disease: a blood-based assay},
  author={Julie Ann Edgeworth and Michael Farmer and Anita Sicilia and Paula Tavares and Jonathan Beck and Tracy A. Campbell and Jessica Lowe and Simon Mead and Peter Rudge and John Collinge and Graham S. Jackson},
  journal={The Lancet},
  year={2011},
  volume={377},
  pages={487-493}
}

Figures from this paper

Preclinical Detection of Prions in Blood of Nonhuman Primates Infected with Variant Creutzfeldt-Jakob Disease

Protein misfolding cyclic amplification (PMCA) has the potential to detect vCJD prions in blood from asymptomatic carriers during the preclinical phase of the disease.

Detection of prions in the plasma of presymptomatic and symptomatic patients with variant Creutzfeldt-Jakob disease

It is shown that a diagnostic assay combining plasminogen-bead capture and protein misfolding cyclic amplification (PMCA) technologies consistently detected minute amounts of abnormal prion protein from French and British vCJD cases in the required femtomolar range.

Preclinical detection of infectivity and disease-specific PrP in blood throughout the incubation period of prion disease

This assay is sensitive for abnormal PrP conformers at the earliest stages of preclinical prion disease in mice and precedes the maximum infectious titre in blood, which supports the possibility of screening asymptomatic individuals and will facilitate the elucidation of the complex relationship that exists between the ensemble of abnormal Prp conformers present in blood and the relationship to infectivity.

Preclinical Detection of Variant CJD and BSE Prions in Blood

Results indicate that the homology of PrP amino-acid sequence between the seed and the substrate is not the crucial determinant of the vCJD agent propagation in vitro, and the ovine Q171 PrP substrates provided the best amplification performances.

Accelerated, Spleen-Based Titration of Variant Creutzfeldt-Jakob Disease Infectivity in Transgenic Mice Expressing Human Prion Protein with Sensitivity Comparable to That of Survival Time Bioassay

The highly sensitive, accelerated spleen-based assay should constitute a key advance for variant CJD epidemiological and risk assessment purposes and should greatly facilitate future titration studies, including, for example, those aimed at validating decontamination procedures.

Plasminogen-Based Capture Combined with Amplification Technology for the Detection of PrPTSE in the Pre-Clinical Phase of Infection

A sensitive and specific amplification assay allowing the detection of PrPTSE in the plasma and buffy coat fractions of blood collected at the pre-clinical phase of the disease.

Distribution and Quantitative Estimates of Variant Creutzfeldt-Jakob Disease Prions in Tissues of Clinical and Asymptomatic Patients

In vitro amplification of prions by protein misfolding cyclic amplification (PMCA) identified major levels of vCJD prions in a range of tissues, including liver, salivary gland, kidney, lung, and bone marrow, which provide critical data for the design of measures to minimize risk for iatrogenic transmission ofvCJD.

In Vitro Detection of prionemia in TSE-Infected Cervids and Hamsters

Modification of the real time quaking-induced conversion (RT-QuIC) assay to detect blood-borne prions in whole blood from prion-infected preclinical white-tailed deer, muntjac deer, and Syrian hamsters is reported, offering promise for prionemia detection in other species, including humans.

Capillary electromigration based techniques in diagnostics of prion protein caused diseases

Assays for prion protein detection are summarized with special attention to capillary electromigration based techniques, such as CE, CIEF, and/or CGE, with the potential of the miniaturized and integrated lab‐on‐chip devices.

White Blood Cell-Based Detection of Asymptomatic Scrapie Infection by Ex Vivo Assays

It is confirmed that white blood cells are appropriate targets for preclinical detection and ex vivo tools to detect blood infectivity during the asymptomatic stage of the disease are introduced.
...

References

SHOWING 1-10 OF 41 REFERENCES

Prion infectivity in variant Creutzfeldt–Jakob disease rectum

These data confirm the potential risks for secondary transmission of vCJD prions via gastrointestinal procedures and support the use of PrPSc as a quantitative marker of prion infectivity in vC JD tissues.

A highly sensitive immunoassay for the detection of prion‐infected material in whole human blood without the use of proteinase K

The best diagnostic tools for vCJD depend upon the detection of disease‐associated prion protein (PrPSc), which is distinguished from normal background PrP (PrPC) by proteinase K (PK) digestion, which can also degrade up to 90% of the target antigen.

Presymptomatic Detection of Prions in Blood

The ability to detect prions biochemically in the blood of infected but not clinically sick animals offers a great promise for the noninvasive early diagnosis of TSEs.

Prevalence of disease related prion protein in anonymous tonsil specimens in Britain: cross sectional opportunistic survey

The observed prevalence of PrPCJD in tonsils from the 1961-95 combined birth cohort was lower than, but still consistent with, a previous survey of appendix tissue that showed a prevalence of 292 per million with a 95% confidence interval of 60 to 853 per million.

Large‐scale immunohistochemical examination for lymphoreticular prion protein in tonsil specimens collected in Britain

Findings could be summarized as finding, by IHC, no or one vCJD‐positive individual.

Prevalence of lymphoreticular prion protein accumulation in UK tissue samples

The findings reinforce the importance of measures taken by the UK Department of Health to reduce the risk of spread of variant Creutzfeldt‐Jakob via blood products and surgical instruments, and of the urgency to proceed with large‐scale screening of fresh tonsil specimens for the presence of prion protein.

Prion diseases of humans and animals: their causes and molecular basis.

The appearance of a novel human prion disease, variant CJD, and the clear experimental evidence that it is caused by exposure to BSE has highlighted the need to understand the molecular basis of prion propagation, pathogenesis, andThe barriers limiting intermammalian transmission.