Journal article
Conservation of a glycine-rich region in the prion protein is required for uptake of prion infectivity
CF Harrison, VA Lawson, BM Coleman, YS Kim, CL Masters, R Cappai, KJ Barnham, AF Hill
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2010
Abstract
Prion diseases are associated with the misfolding of the endogenously expressed prion protein (designated PrPC) into an abnormal isoform (PrPSc) that has infectious properties. The hydrophobic domain of PrPC is highly conserved and contains a series of glycine residues that show perfect conservation among all species, strongly suggesting it has functional and evolutionary significance. These glycine residues appear to form repeats of the GXXXG protein-protein interaction motif (two glycines separated by any three residues); the retention of these residues is significant and presumably relates to the functionality of PrPC. Mutagenesis studies demonstrate that minor alterations to this highly ..
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Awarded by Australian Research Council
Awarded by National Health and Medical Research Council
Funding Acknowledgements
This work was supported in part by Australian Research Council Discovery Project Grant DP0987227 and National Health and Medical Research Council Program Grant 400202.Recipient of an Australian postgraduate award scholarship.Recipient of a University of Melbourne CR Roper fellowship.Recipient of a University of Melbourne research scholarship.Recipient of a National Health and Medical Research Council senior research fellowship.Recipient of National Health and Medical Research Council career development award (Level 2). A shareholder in and consultant to D-Gen Limited, an academic spin-out company working in the field of prion disease diagnosis, therapeutics, and decontamination. D-Gen markets the ICSM18 antibody used in this study.