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Preface—Prion Research in Perspective III

“Prion Research in Perspective III” is PrioNet Canada’s third open paper call, and its mandate continues to give PrioNet Canada, the Alberta Prion Research Institute, and other partner organization researchers a venue to publish their latest research. In total, 14 papers were accepted after peer review. The papers contribute to one or more of PrioNet Canada’s three research themes: Prion Biology, Prion Ecology, and Prion Prevention and Preparedness. Papers accepted were of two types, either full-length manuscripts or shorter brevia-type manuscripts. The latter category is targeted to encourage the participation of students and highly qualified personnel. PrioNet continues its commitment to foster the development of young researchers in Canada. The lead paper by Guest et al. (Cashman Laboratory) provides an overview of the expanding field of prion-like diseases. Increasing evidence links a prion-like process in the propagation of several neurodegenerative diseases, including Alzheimer’s, Parkinson’s, Huntington’s, amyotrophic lateral sclerosis, and tauopathies. Guest et al. provide a succinct review of the mechanisms of protein misfolding and aggregation for neurodegenerationassociated proteins, focusing on the hypothesis that released microvesicles function as misfolded protein delivery vehicles. Because Dr. Cashman is one of the special issue guest editors, his contribution was handled by the journal’s editor-in-chief, Dr. Sam Kacew, and guest editor Dr. Michael Tyshenko. The second paper in the Prion Biology theme is by Lukiw et al. (Lukiw Laboratory), who investigated the upregulation of micro RNA-146a (miRNA-146a) as a marker for inflammatory neurodegeneration. The authors contend that upregulated miRNA-146a may be integral to innate immune or inflammatory brain cell responses in prion-mediated infections in sporadic Creutzfeldt–Jakob disease (sCJD) and Gerstmann–Straussler–Scheinker (GSS) syndrome. In the third paper, Dvorakova et al. (Holada Laboratory) discuss the development and potential use of monoclonal antibodies specific for glycated prion protein. Besides the obvious application for transmissible spongiform encephalopathy (TSE) diagnostics, the antibodies may help advance knowledge about the role of glycation in prion pathophysiology. The fourth paper, by Pushie et al. (Vogel Laboratory), presents an interesting nuclear magnetic resonance (NMR) metabolomics study of elk inoculated with chronic wasting disease (CWD). The research is of great interest as it could help identify key biomarkers of disease incubation. The fifth paper, by Zhou et al. (Zou Laboratory), provides details of the alkylating antitumor drug mechlorethamine that inhibits in vitro prion amplification by concealing a structured PrP domain. Much work remains to be completed to realize this as a therapeutic agent for treating prion diseases, but the result suggests a possible potential application. The sixth and final paper in the Prion Biology theme, by Huzarewich et al. (Booth Laboratory), looks at the transcriptional modulation in a leukocyte-depleted splenic cell population during prion disease. The alteration of gene expression of these cells may lead to the identification of potential surrogate markers for prion disease pathogenesis. Only one paper was submitted in the Prion Ecology theme, by Rogers et al. (Samuel