有哪些信誉好的足球投注网站a new method for the characterization of strain-specific conformational stability of protease-sensitive and protease-resistant prpsc特性的一种新方法毒株特异性protease-sensitive和protease-resistant朊蛋白的构象稳定.pdfVIP
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a new method for the characterization of strain-specific conformational stability of protease-sensitive and protease-resistant prpsc特性的一种新方法毒株特异性protease-sensitive和protease-resistant朊蛋白的构象稳定
A New Method for the Characterization of Strain-Specific
Conformational Stability of Protease-Sensitive and
Protease-Resistant PrPSc
1 1 1 1 1 1
Laura Pirisinu , Michele Di Bari , Stefano Marcon , Gabriele Vaccari , Claudia D’Agostino , Paola Fazzi ,
1 2 3 1 1
Elena Esposito , Roberta Galeno , Jan Langeveld , Umberto Agrimi , Romolo Nonno *
`
1 Department of Veterinary Public Health and Food Safety, Istituto Superiore di Sanita, Rome, Italy, 2 Department of Cell Biology and Neurosciences, Istituto Superiore di
`
Sanita, Rome, Italy, 3 Central Veterinary Institute, Wageningen UR, Lelystad, The Netherlands
Abstract
Although proteinacious in nature, prions exist as strains with specific self-perpetuating biological properties. Prion strains
are thought to be associated with different conformers of PrPSc, a disease-associated isoform of the host-encoded cellular
protein (PrPC). Molecular strain typing approaches have been developed which rely on the characterization of protease-
resistant PrPSc. However, PrPSc is composed not only of protease-resistant but also of protease-sensitive isoforms. The aim of
this work was to develop a protocol for the molecular characterization of both, protease-resistant and protease-sensitive
PrPSc aggregates. We first set up experimental conditions which allowed the most advantageous separation of PrPC and
PrPSc by means of differential centrifugation. The conformational solubility and stability assay (CSSA) was then developed by
measuring PrPSc solubility as a function of increased expos
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