Immunodiagnosis of Prion Disease

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Abstract
Strlusler syndrome, kuru and fatal familial insomnia. Recently this group of disorders has spread to new hosts including cattle and domestic cats. While these conditions occur at a lowfrequency, diagnosis is important because of their transmissibility and fatal prognosis. The hallmark of these disorders is the conversion of a host membrane glycoprotein termed PrP" {or PrP'en} into a protease resistant highly aggregated form termed Prplic { or PrP"'"} (3). Mutation in the gene which codes for this protein in the form of point mutations, insertions and deletions are associated with genetically inherited forms of these diseases (4). The majority of human prion diseases (greater than 95% of cases) occur sporadically with no known source of infection. The only known contributing factor is a higher incidence ofdisease associated with homozygosity for a polymorphism at codon 129 of the PrP gene (5). The rapid and accurate diagnosis of prion diseases is of critical importance to themedical communities. The immunological detection of PrP using either monoclonal orpolyclonal antibodies to PrP affords the sensitivity and specificity required for such an assay.