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The pathogenesis of TSEs involves conformational conversions of normal cellular PrP (PrP<jats:sup>c<\/jats:sup>) to abnormal isoforms of PrP (PrP<jats:sup>Sc<\/jats:sup>). While the protein-only hypothesis has been widely accepted as a causal mechanism of prion diseases, evidence from more recent research suggests a possible involvement of other cellular component(s) or as yet undefined infectious agent(s) in PrP pathogenesis. Although the underlying mechanisms of PrP strain variation and the determinants of interspecies transmissibility have not been fully elucidated, biochemical and molecular findings indicate that bovine spongiform encephalopathy in cattle and new-variant Creutzfeldt\u2013Jakob disease in humans are caused by indistinguishable etiological agent(s). Cumulative evidence suggests that there may be risks of humans acquiring TSEs via a variety of exposures to infected material. The development of highly precise ligands is warranted to detect and differentiate strains, allelic variants and infectious isoforms of these PrPs. This article describes the general features of TSEs and PrP, the current understanding of their pathogenesis, recent advances in prion disease diagnostics, and PrP inactivation.<\/jats:p>","DOI":"10.1079\/ahr200494","type":"journal-article","created":{"date-parts":[[2005,7,4]],"date-time":"2005-07-04T01:41:09Z","timestamp":1120441269000},"page":"103-124","update-policy":"http:\/\/dx.doi.org\/10.1017\/policypage","source":"Crossref","is-referenced-by-count":8,"title":["An overview of transmissible spongiform 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