Home Acta Virologica 2006 Acta Virologica Vol.50, p.25-32, 2006

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Founded: 1957
ISSN 0001-723X
E-ISSN 1336-2305

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Acta Virologica Vol.50, p.25-32, 2006

Title: INFLUENCE OF GUANIDINE ON PROTEINASE K RESISTANCE IN VITRO AND INFECTIVITY OF SCRAPIE PRION PROTEIN PRPSc
Author: J.M. GAO, X.B. ZHOU, X.L. XIAO, J. ZHANG, L. CHEN, C. GAO, B.Y. ZHANG, X.P. DONG

Abstract: As the scrapie prion protein PrPSc is rich in ß-sheets it aggregates into prion rods, which show infectivity and proteinase K (PK) resistance. Consequently, dissociation of prion rods and breakdown of β-sheets in PrPSc by denaturation results in loss of both infectivity and PK-sensitivity. In this study, the effects of guanidine (Gdn), which solubilizes and denatures proteins by breaking down their higher structure, on the solubility, the PK-resistance in vitro and the infectivity of PrPSc of scrapie strain 263K was examined. The infectivity was assayed by intracerebral inoculation into hamsters. Brain tissues of scrapie-infected hamsters were used for preparation of homogenates and crude extracts of PrPSc. A treatment of PrPSc with Gdn enhanced its PK-sensitivity in a dosedependent manner. The PK-resistance in vitro of PrPSc denatured with lower concentrations of Gdn (<2.5 mol/l) could partially resume by renaturation. Gdn markedly reduced or, at higher concentrations, even destroyed the infectivity of PrPSc. On the other hand, the infectivity of PrPSc inactivated by denaturation could be partially restored by renaturation. These results confirmed our assumption that all the alternations in the PK-resistance and the infectivity of PrPSc caused by Gdn resulted from changes in its higher structure. However, it should be emphasized that a complete loss of PK-resistance of PrPSc may not necessarily mean its full non-infectivity.

Keywords: scrapie; prions; PrPSc; guanidine; proteinase K; infectivity
Year: 2006, Volume: 50, Issue: Page From: 25, Page To: 32



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