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Post-conversion sialylation of prions in lymphoid tissues
Saurabh Srivastava1, Natallia Makarava1, Elizaveta Katorcha1
1Center for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, MD 21201; Department of Anatomy and Neurobiology, University of Maryland School of Medicine, Baltimore, MD 21201;
Summary
Prions change their sialylation status in lymphoid organs, becoming more sialylated. This host-driven modification may help prions camouflage themselves from the immune system.
Area of Science:
- Neuroscience
- Immunology
- Biochemistry
Background:
- Sialylated glycans on cell surfaces help the immune system distinguish 'self' from 'non-self'.
- Bacterial pathogens mimic or utilize host sialic acids to evade immune detection.
- Prions, unconventional pathogens lacking nucleic acids, may employ similar immune evasion strategies.
Purpose of the Study:
- To investigate if the sialylation status of the prion protein (PrP(Sc)) changes during colonization of secondary lymphoid organs (SLOs).
- To explore the role of host sialyltransferases (STs) in altering PrP(Sc) sialylation.
- To determine if altered sialylation contributes to prion camouflage in SLOs.
Main Methods:
- Comparison of sialylation status of PrP(Sc) from spleen versus brain tissue.
- In vitro incubation of brain-derived PrP(Sc) with primary splenocytes and RAW 264.7 macrophages.
- Treatment with sialyltransferase inhibitors to assess their effect on PrP(Sc) sialylation.
- Detection of sialyltransferase activity in macrophages using fluorescently labeled sialic acid precursors.
Main Results:
- Spleen-derived PrP(Sc) exhibited higher sialylation compared to brain-derived PrP(Sc).
- Incubation with splenocytes or macrophages enhanced PrP(Sc) sialylation in vitro.
- Sialyltransferase inhibitors reduced the extrasialylation of PrP(Sc).
- Macrophages demonstrated sialyltransferase activity.
Conclusions:
- Prion colonization of SLOs leads to changes in PrP(Sc) sialylation mediated by host sialyltransferases.
- This enhanced sialylation likely serves as a camouflage mechanism for prions within SLOs.
- The findings have broad implications for understanding prion pathogenesis and host-pathogen interactions.
