Abstract
Prion diseases are transmissible fatal neurodegenerative disorders affecting humans and animals. A central step in disease progression is the accumulation of a misfolded form (PrPSc) of the host encoded prion protein (PrPC) in neuronal and non-neuronal tissues. The involvement of peripheral tissues in preclinical states increases the risk of accidental transmission. On the other hand, detection of PrPSc in non-neuronal easy-accessible compartments such as muscle may offer a novel diagnostic tool. Primate models have proven invaluable to investigate prion diseases. We have studied the deposition of PrPSc in muscle and central nervous system of rhesus monkeys challenged with sporadic Creutzfeldt-Jakob disease (sCJD), variant CJD (vCJD) and bovine spongiform encephalopathy (BSE) in preclinical and clinical stage using biochemical and morphological methods. Here, we show the preclinical presence of PrPSc in muscle and central nervous system of rhesus monkeys experimentally infected with vCJD.
Highlights
Prion diseases are transmissible neurodegenerative disorders characterized by neuronal loss, astrocytosis and deposition of the pathogenic isoform (PrPSc) of the cellular prion protein (PrPC)
Genetic Creutzfeldt-Jakob disease co-segregates with mutations in the gene encoding the prion protein and is inherited autosomal dominantly [11], whereas acquired forms are caused by exposure to infectious human prions during medical or neurosurgical procedures or a non-human prion source such as bovine spongiform encephalopathy (BSE)-prions [12]
To investigate if intraperitoneal prion inoculation leads to the development of clinical prion disease, we infected rhesus monkeys with variant CJD (vCJD), Sporadic Creutzfeldt-Jakob disease (sCJD) and BSE-prions or saline intraperitoneally
Summary
Prion diseases are transmissible neurodegenerative disorders characterized by neuronal loss, astrocytosis and deposition of the pathogenic isoform (PrPSc) of the cellular prion protein (PrPC). Human prion diseases include sporadic, genetic and acquired forms [7,8]. Interhuman transmission of vCJD through blood transfusions has occurred in several instances [6,13]. No such transmissions have been reported with other human prion diseases such as sCJD. This demonstrates that peripheral tissues of vCJD infected individuals harbouring relatively low prion titer may lead to prion transmission following host-adaption
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