A new variant of prion disease

doi:10.1016/S0140-6736(96)91407-5

The Lancet

Volume 347, Issue 9006, 6 April 1996, Pages 916-917

https://doi.org/10.1016/S0140-6736(96)91407-5 Get rights and content

References (7)

Pem Smith et al.
Creutzfeldt-Jakob disease in a dairy farmer
Lancet
(1995)
Tc Britton et al.
Sporadic Creutzfeldt-Jakob disease in a 16-year-old in the UK
Lancet
(1995)
D. Bateman et al.
Sporadic Creutzfeldt-Jakob disease in a 18-year-old in the UK
Lancet
(1995)

There are more references available in the full text version of this article.

Cited by (80)

Prion diseases
2022, European Neuropsychopharmacology
Region-specific protein misfolding cyclic amplification reproduces brain tropism of prion strains
2017, Journal of Biological Chemistry
Citation Excerpt :
Recently, some sCJD subtypes have been associated with distinct human prion strains by transmission to nonhuman primates and transgenic mice (5, 6). A higher proportion of diglycosylated forms characterizes the type 2b PrPSc that is found in variant CJD (vCJD), which results from the cattle to human transmission of the prion strain responsible for the epizootic bovine spongiform encephalopathy (BSE) (9). vCJD is associated with a particular involvement of the posterior thalamus (10).
Human prion diseases such as Creutzfeldt-Jakob disease are transmissible brain proteinopathies, characterized by the accumulation of a misfolded isoform of the host cellular prion protein (PrP) in the brain. According to the prion model, prions are defined as proteinaceous infectious particles composed solely of this abnormal isoform of PrP (PrP^Sc). Even in the absence of genetic material, various prion strains can be propagated in experimental models. They can be distinguished by the pattern of disease they produce and especially by the localization of PrP^Sc deposits within the brain and the spongiform lesions they induce. The mechanisms involved in this strain-specific targeting of distinct brain regions still are a fundamental, unresolved question in prion research. To address this question, we exploited a prion conversion in vitro assay, protein misfolding cyclic amplification (PMCA), by using experimental scrapie and human prion strains as seeds and specific brain regions from mice and humans as substrates. We show here that region-specific PMCA in part reproduces the specific brain targeting observed in experimental, acquired, and sporadic Creutzfeldt-Jakob diseases. Furthermore, we provide evidence that, in addition to cellular prion protein, other region- and species-specific molecular factors influence the strain-dependent prion conversion process. This important step toward understanding prion strain propagation in the human brain may impact research on the molecular factors involved in protein misfolding and the development of ultrasensitive methods for diagnosing prion disease.
Neuroepidemiology and the epidemiology of viral infections of the nervous system
2014, Handbook of Clinical Neurology
Citation Excerpt :
However, despite the millions of neurosurgeries performed each year, there have been only a handful of documented cases of CJD being associated with contaminated neurosurgical instruments or implanted electroencephalogram electrodes. Beginning in 1995, several cases of CJD with atypical features were noted in the United Kingdom; these cases had illness onset at a much younger age (mean age at onset of 26 years), a longer duration of illness before death, and atypical initial symptoms, including psychiatric manifestations and prominent sensory disturbances (Collinge and Rossor, 1996; Will et al., 1996). Early on, a link between this “new variant” CJD (now variant CJD, vCJD) and BSE in cattle was suspected, based upon several lines of epidemiologic and pathologic data, and suggested transmission of the BSE prion agent from cattle to humans (Collinge, 1997).
Viral infections result in a tremendous burden of neurologic illness worldwide. Although many viral etiologies of neurologic infectious disease have been recently controlled through vaccination and other public health measures, the emergence of new pathogens and the re-emergence of previously controlled pathogens remain significant global public health challenges. One of the fundamental bases for understanding the dynamics of viral nervous system infections is through epidemiology – the science of assessing patterns of disease in populations and the factors that influence these patterns. Neuroepidemiology is a discipline that applies epidemiologic principles and practices to neurologic disease. There are several characteristics of neurologic illness that necessitate the subdiscipline of neuroepidemiology. This chapter reviews some of the basic terms and concepts of neuroepidemiology, including epidemiologic analysis and studies. It then applies these concepts to infections of the nervous system, including encephalitis, aseptic meningitis, acute myelitis, prion diseases, and slow virus infections. The chapter then addresses the epidemiology of emerging and re-emerging viral neurologic diseases as well as the factors driving these emergences. The epidemiology of viral nervous system diseases will undoubtedly continue to change and expand, and as we gain a better understanding of this epidemiology and the pathophysiology of viral infections, this will hopefully lead to improved surveillance, diagnostic, treatment, and prevention strategies for these illnesses.
Creutzfeldt-jakob disease
2013, Continuing Education in Anaesthesia, Critical Care and Pain
Citation Excerpt :
The first cases of vCJD were reported in 1995, 12 years after the identification of BSE.3,4 However, as more cases were identified, atypical clinical and pathological features were described, and this new disease was named new vCJD.5 The peak of the epidemic is likely to have been in 2000, which gives an estimate of an incubation period based on BSE to vCJD peaks of 8 years.
Comparative performance of three TSE rapid tests for surveillance in healthy sheep affected by scrapie
2011, Journal of Virological Methods
Citation Excerpt :
Although scrapie has occurred in the European small ruminant population for more than 200 years, making it a well-established endemic disease, it has never been associated with human forms of the disease. However, BSE has been shown to be zoonotic (Bruce et al., 1997; Collinge and Rossor, 1996; Will, 1998) and has been experimentally transmitted in both sheep and goats (Foster et al., 1993). It is thought that sheep and possibly goats were exposed to BSE contaminated meat and bone meal in the early 1980s and the concern has been that BSE may be sustained in sheep populations and so represent a secondary risk to human health.
Rapid tests specific for sheep and goats became part of European Union-wide active scrapie surveillance in 2006. Performance of three approved TSE rapid tests for the detection of sheep infected with scrapie in field cases in the pre-clinical stage of the disease was compared.
The medulla oblongata of 969 asymptomatic sheep of various genotype and breed aged over 18 months from 23 Italian flocks affected with scrapie, were tested by the Bio-Rad TeSeE Sheep/Goat (A), the IDEXX HerdChek BSE-Scrapie Antigen Test Kit, EIA (B) and the Prionics^®-Check Western Small Ruminant (C) rapid tests.
Of 136 positive samples of classical scrapie, as confirmed by Western blot assay, 132 were positive with test A (Se 97.06%, CI 95% 92.64–99.19); 135 with test B (Se 99.26%, 95% CI 95.97–99.98) and 128 with test C (Se 94.12%, 95% CI 88.74–97.43).
Tests A and B showed the best performance on analytical sensitivity. All three systems demonstrated good reproducibility: being the intrarater and interrater kappa coefficients always over 0.83.
The one available atypical scrapie sample was positive with tests A and B, negative with test C.
Considering the discrepant results in the detection of low PrP^sc concentrations and of the atypical case, differences can be expected in the efficacy of an active surveillance system, depending on the test adopted.
Cells and prions: A license to replicate
2009, FEBS Letters
Prion diseases are neurodegenerative, infectious disorders characterized by the aggregation of a misfolded isoform of the cellular prion protein (PrP^C). The infectious agent – termed prion – is mainly composed of misfolded PrP^Sc. In addition to the central nervous system prions can colonize secondary lymphoid organs and inflammatory foci. Follicular dendritic cells are important extraneural sites of prion replication. However, recent data point to a broader range of cell types that can replicate prions. Here, we review the state of the art in regards to peripheral prion replication, neuroinvasion and the determinants of prion replication competence.

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COMMENTARYA new variant of prion disease

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A new variant of prion disease