The pathogen slow virus virino or prion

In the late 1940s, Wilson at the Moredun Institute, Edinburgh, classified the scrapie agent as a virus, based on filtration studies through membranes, and, in 1954, Sigurdsson included rida (Icelandic scrapie) with maedi/visna and infectious adenomatosis in his group of slow virus diseases. These diseases were shown to be caused by conventional viruses but the molecular structure of the TSE pathogen remains a subject for debate. While it has some of the properties of a conventional virus, such as strain variation and mutation, others, such as surviving virucidal procedures, lend credence to the hypothesis that a host protein, PrP or prion protein, may be transformed into the infectious particle. Prion, slow virus and virino are all used as synonyms for the causative agent of TSE diseases: a virino is a composite structure of host protein (possibly PrP) and a host-independent molecule (possibly nucleic acid) which determines the strain of scrapie; a slow virus is a conventional structure of host-independent protein and nucleic acid; and one version of the prion structure has some form of PrP as the sole component of the scrapie pathogen. In all of these diseases PrP accumulates abnormally in the brain and this isoform (PrPv or PrP-res) copurifies with infectivity. In some TSEs, PrPSc can also be identified in extracts from peripheral tissues (e.g. spleen, lymph nodes). Anti-PrP antibodies do not neutralize infectivity and no autoantibodies to PrP have been detected in the sera or cerebrospinal fluid of affected animals or man.

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