Prions,proteinase K and infectivity |
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Authors: | Gustavo Sajnani Jesús R Requena |
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Affiliation: | 1.Neural Repair and Biomaterials Laboratory; National Paraplegia Hospital; Finca la Peraleda s/n; Toledo, Spain;2.CIMUS Biomedical Research Institute; University of Santiago de Compostela-IDIS; Santiago de Compostela, Spain;3.Department of Medicine; University of Santiago de Compostela-IDIS; Santiago de Compostela, Spain |
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Abstract: | It has been described that the breakdown of β-sheets in PrPSc by denaturation results in loss of infectivity and PK-sensitivity, suggesting a relationship between the structure and PK-resistance. It is also known that an important fraction of total PrPSc is PK-sensitive and can be isolated by the method we already described. Consequently, we decided to employ the PK-sensitive fraction of PrPSc as a potential and useful tool for structural studies. Thus, two essential questions were addressed in our recent article. First, the difference in the infectivity between the sensitive and resistant fractions and second, whether sensitive and resistant PrPSc shared the same conformation or were only different size multimers with the same basic conformation. Here we discuss our latest data in light of recent infectivity studies and their possible implications on the conformation of the prion. |
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Keywords: | prion sensitive PrPSc resistant PrPSc infectivity structure |
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