Abstract
Transmissible spongiform encephalopathy (TSE) agents also named prions are responsible for transmissible subacute spongiform encephalopathies in humans and animals. TSE agents are thought to be composed only of an abnormal isoform of a host-coded protein, the prion protein (PrP). In vivo, raise in infectivity titer is always associated with a proportional accumulation of PrP. Aminoacid sequences of PrP obtained from normal and infected brains are identical, and these two proteins differ only by their biochemical and biophysical behaviour: in particular, PrP from TSE-affected individuals resists to proteinase K digestion. PrP-c is the PrP found in normal individuals, PrP-res is the proteinase K resistant PrP identifiable in infected individuals. TSE agents are capable to cross the species barrier. In march 96, a new variant of Creutzfeldt-Jakob disease (vCJD) has been described in UK. This emerging disease is now recognized to be induced by the BSE agent. Protection of human health is ensured by systematic PrP-res screening of cattle at slaughterhouse and by the specified risk material ban in the human and animal food chain.
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