Abstract
Recent years witnessed extraordinary rise of interest to sialylation and, specifically, to its role in host–pathogen interactions. Prions or PrPSc are proteinaceous infectious agents that consist of misfolded, aggregated, self-replicating states of a sialoglycoprotein called the prion protein or PrPC. Prions are not conventional pathogens. Nevertheless, due to sialylation of N-linked glycans, prions may use mechanisms similar to those exploited by microbial or viral pathogens in invading a host. Recent studies revealed that sialylation of PrPSc controls prion infectivity, replication rate, and strain-specific glycoform ratios. As such, sialylation is of paramount importance to prion pathogenesis. For assessing sialylation status of PrPSc, we developed reliable protocol that involves two-dimensional electrophoresis followed by Western blot (2D). The current chapter describes the procedure for analysis of sialylation status of PrPSc from various sources including brain, spleen, cultured cells, or Protein Misfolding Cyclic Amplification using 2D.
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This work was supported by the National Institute of Health grant R01 NS045585.
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Katorcha, E., Baskakov, I.V. (2017). Analysis of Charge Isoforms of the Scrapie Prion Protein Using Two-Dimensional Electrophoresis. In: Liberski, P. (eds) Prion Diseases. Neuromethods, vol 129. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7211-1_11
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DOI: https://doi.org/10.1007/978-1-4939-7211-1_11
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