Schistosome-derived omega-1 drives Th2 polarizationm by suppressing protein 
synthesis following internalization by the mannose receptor

Everts, Bart; Hussaarts, Leonie; Driessen, Nicole N.; Meevissen, Moniek H.J.; Schramm, Gabriele; van der Ham, Alwin J.; van der Hoeven, Barbara; Scholzen, Thomas; Burgdorf, Sven; Mohrs, Markus; Pearce, Edward J.; Hokke, Cornelis H.; Haas, Helmut; Smits, Hermelijn H.; Yazdanbakhsh, Maria

doi:10.1084/jem.20111381

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Schistosome-derived omega-1 drives Th2 polarizationm by suppressing protein synthesis following internalization by the mannose receptor

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Pearce, Edward J.
Department Immunometabolism, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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https://rupress.org/jem/article/209/10/1753/54614/Schistosome-derived-omega-1-drives-Th2
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Citation

Everts, B., Hussaarts, L., Driessen, N. N., Meevissen, M. H., Schramm, G., van der Ham, A. J., et al. (2012). Schistosome-derived omega-1 drives Th2 polarizationm by suppressing protein synthesis following internalization by the mannose receptor. Journal of Experimental Medicine, 209, 1753-1767. doi:10.1084/jem.20111381.

Cite as: https://hdl.handle.net/21.11116/0000-0006-BECF-C

Abstract

Omega-1, a glycosylated T2 ribonuclease (RNase) secreted by Schistosoma mansoni eggs and abundantly present in soluble egg antigen, has recently been shown to condition dendritic cells (DCs) to prime Th2 responses. However, the molecular mechanisms underlying this effect remain unknown. We show in this study by site-directed mutagenesis of omega-1 that both the glycosylation and the RNase activity are essential to condition DCs for Th2 polarization. Mechanistically, we demonstrate that omega-1 is bound and internalized via its glycans by the mannose receptor (MR) and subsequently impairs protein synthesis by degrading both ribosomal and messenger RNA. These experiments reveal an unrecognized pathway involving MR and interference with protein synthesis that conditions DCs for Th2 priming.