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Prions in Variably Protease-Sensitive Prionopathy: An Update
Department of Pathology Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA
Department of Neurology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA
National Prion Disease Pathology Surveillance Center, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA
National Center for Regenerative Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA
The First Affiliated Hospital, Nanchang University, Nanchang 330006, Jiangxi Province, China
State Key Laboratory for Infectious Disease Prevention and Control, National Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100050, China
Central Veterinary Institute of Wageningen UR, Lelystad 8200 AB, the Netherlands
Department of Veterinary Public Health and Food Safety, Istituto Superiore di Sanità, Viale Regina Elena 299 00161, Rome, Italy
* Author to whom correspondence should be addressed.
Received: 12 June 2013; in revised form: 28 June 2013 / Accepted: 2 July 2013 / Published: 5 July 2013
(This article belongs to the Special Issue Prions
Abstract: Human prion diseases, including sporadic, familial, and acquired forms such as Creutzfeldt-Jakob disease (CJD), are caused by prions in which an abnormal prion protein (PrPSc) derived from its normal cellular isoform (PrPC) is the only known component. The recently-identified variably protease-sensitive prionopathy (VPSPr) is characterized not only by an atypical clinical phenotype and neuropathology but also by the deposition in the brain of a peculiar PrPSc. Like other forms of human prion disease, the pathogenesis of VPSPr also currently remains unclear. However, the findings of the peculiar features of prions from VPSPr and of the possible association of VPSPr with a known genetic prion disease linked with a valine to isoleucine mutation at residue 180 of PrP reported recently, may be of great importance in enhancing our understanding of not only this atypical human prion disease in particular, but also other prion diseases in general. In this review, we highlight the physicochemical and biological properties of prions from VPSPr and discuss the pathogenesis of VPSPr including the origin and formation of the peculiar prions.
Keywords: prions; prion protein; prion disease; Creutzfeldt-Jakob disease (CJD); variably protease-sensitive prionopathy (VPSPr); Gerstmann-Sträussler-Scheinker (GSS); mutation; proteinase K; antibody; glycosylation; glycoform-selective prion formation; transmissibility
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Zou, W.-Q.; Gambetti, P.; Xiao, X.; Yuan, J.; Langeveld, J.; Pirisinu, L. Prions in Variably Protease-Sensitive Prionopathy: An Update. Pathogens 2013, 2, 457-471.
Zou W-Q, Gambetti P, Xiao X, Yuan J, Langeveld J, Pirisinu L. Prions in Variably Protease-Sensitive Prionopathy: An Update. Pathogens. 2013; 2(3):457-471.
Zou, Wen-Quan; Gambetti, Pierluigi; Xiao, Xiangzhu; Yuan, Jue; Langeveld, Jan; Pirisinu, Laura. 2013. "Prions in Variably Protease-Sensitive Prionopathy: An Update." Pathogens 2, no. 3: 457-471.