Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins.

Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins.

The central event in prion infection is the conformational conversion of host-encoded cellular prion protein (PrP(C)) into the pathogenic isoform (PrP(Sc)). Diverse mammalian species possess the cofactors required for in vitro replication of PrP(Sc) by protein-misfolding cyclic amplification (PMCA),...

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Bibliographic Details
Main Authors: Morikazu Imamura, Nobuko Kato, Hiroyuki Okada, Miyako Yoshioka, Yoshifumi Iwamaru, Yoshihisa Shimizu, Shirou Mohri, Takashi Yokoyama, Yuichi Murayama
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3867355?pdf=render

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http://europepmc.org/articles/PMC3867355?pdf=render

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