title: Relation between duration of incubation period of prion infections and prion protein conformation.
abstract: In this paper, we propose the hypothesis that the long incubation period of prion infections is dependent upon a low rate of pathological prion formation and accumulation. Reduced pathological prion formation might be caused by the high content of β-sheets in the molecule. β-Sheet folding appears to proceed more slowly than folding of α-helices; the former are a major component of the prion secondary structure. This hypothesis strongly agrees with the data about folding of the artificial protein l-polylysine. This protein exists in two subforms: a rapidly folding α-helix-enriched form and a β-sheet-rich form having a very slow speed of secondary and tertiary structure formation. According to our hypothesis, the limiting factor for prion infection propagation is the speed of β-sheet folding in molecules of pathological prion but not the speed of migration of this protein through the host organism.
authors.affiliation: Scientific Center for Prion Infections Study, Institute of Animal Biology UAAS, 38 Stusa Str., Lviv 79034, Ukraine. vitalii.stadnyk@yahoo.com
authors.forename: Vitalii
authors.initials: V
authors.lastname: Stadnyk
authors.forename: Chrystyna
authors.initials: C
authors.lastname: Mayor
authors.forename: Lyudmyla
authors.initials: L
authors.lastname: Izyumova
authors.forename: Vasyl
authors.initials: V
authors.lastname: Vlizlo
mesh_terms: D000818:Animals; D006801:Humans; D055256:Infectious Disease Incubation Period; D008954:Models, Biological; D017096:Prion Diseases / Q000503:physiopathology*; D011328:Prions / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D011328:Prions