Abstract
Twenty-five years has now passed since variant Creutzfeldt-Jakob disease (vCJD) was first described in the United Kingdom (UK). Early epidemiological, neuropathological and biochemical investigations suggested that vCJD represented a new zoonotic form of human prion disease resulting from dietary exposure to the bovine spongiform encephalopathy (BSE) agent. This hypothesis has since been confirmed though a large body of experimental evidence, predominantly using animal models of the disease. Today, the clinical, pathological and biochemical phenotype of vCJD is well characterized and demonstrates a unique and remarkably consistent pattern between individual cases when compared to other human prion diseases. While the numbers of vCJD cases remain reassuringly low, with 178 primary vCJD cases reported in the UK and a further 54 reported worldwide, concerns remain over the possible appearance of new vCJD cases in other genetic cohorts and the numbers of asymptomatic individuals in the population harboring vCJD infectivity. This review will provide a historical perspective on vCJD, examining the origins of this acquired prion disease and its association with BSE. We will investigate the epidemiology of the disease along with the unique clinicopathological and biochemical phenotype associated with vCJD cases. Additionally, this review will examine the impact vCJD has had on public health in the UK and the ongoing concerns raised by this rare group of disorders.
Highlights
Prion diseases or transmissible spongiform encephalopathies (TSEs) are a group of rare neurodegenerative conditions that occur naturally in humans as well as a range of animal species
Twenty-five years has passed since the first description of variant Creutzfeldt-Jakob disease (vCJD) in the United Kingdom (UK)
Case numbers in the UK and worldwide remain relatively low with 232 clinical cases of definite or probable vCJD reported to date
Summary
Prion diseases or transmissible spongiform encephalopathies (TSEs) are a group of rare neurodegenerative conditions that occur naturally in humans as well as a range of animal species. Human prion diseases share many clinical and neuropathological features with that of more common neurodegenerative conditions such as Alzheimer’s disease and Parkinson’s disease, in particular the accumulation in the brain of abnormal, disease-specific protein aggregates [1]. In prion diseases, this protein is a misfolded and partially protease-resistant form of a normal host-encoded cellular protein, the prion protein (PrPC ) [2,3,4]. As a consequence of this infectious nature, prion diseases represent a neurodegenerative condition that poses a serious public health concern. We will detail the public health impact following the identification of vCJD in the UK and the current public health concerns that still surround this condition a quarter of a century on
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