Cited by 236Parasites and Host InteractionsImmunotherapy and Immune ResponsesParasitic Diseases Research and Treatment
Schistosome-derived omega-1 drives Th2 polarization by suppressing protein synthesis following internalization by the mannose receptor
Open accessEverts, Bart, Hussaarts, Leonie, Driessen, Nicole N., Meevissen, Moniek H.J., Schramm, Gabriele, van der Ham, Alwin J., van der Hoeven, Barbara, Scholzen, Thomas +7 more·2012·Journal of Experimental Medicine
DOI 10.1084/jem.20111381PMC PMC3457738
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.
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The functionality of the T2 ribonuclease family may have evolved within the trematode family relatively recently.
“Conversely, expansion of the T2 ribonuclease family (containing omega-1) (Everts et al., 2012) appears specific to schistosomes (Figure 4C), implying that this functionality may have evolved within the trematode family relatively recently.”
From Modulation of Host Immunity by Helminths: The Expanding Repertoire of Parasite Effector Molecules (2018) · cites this paper as Everts et al., 2012
Expansion of the T2 ribonuclease family, containing omega-1, appears specific to schistosomes.
“Conversely, expansion of the T2 ribonuclease family (containing omega-1) (Everts et al., 2012) appears specific to schistosomes (Figure 4C), implying that this functionality may have evolved within the trematode family relatively recently.”
From Modulation of Host Immunity by Helminths: The Expanding Repertoire of Parasite Effector Molecules (2018) · cites this paper as Everts et al., 2012
This latter function appears to have been utilized in schistosomes, degrading RNA in host dendritic cells and suppressing their maturation.
“and it is this latter function which appears to have been utilized in the schistosomes, degrading RNA in host DCs and suppressing their maturation (Everts et al., 2012).”
From Modulation of Host Immunity by Helminths: The Expanding Repertoire of Parasite Effector Molecules (2018) · cites this paper as Everts et al., 2012
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Modulation of Host Immunity by Helminths: The Expanding Repertoire of Parasite Effector Molecules
Maizels, R. M., Smits, H. H., & McSorley, H. J. (2018) · Immunity · doi:10.1016/j.immuni.2018.10.016 · Cited by 435 · see citing works
Self-citation
- Authors
- Everts, B., Hussaarts, L., Driessen, N. N., Meevissen, M. H. J., Schramm, G., van der Ham, A. J., van der Hoeven, B., Scholzen, T., Burgdorf, S., Mohrs, M., Pearce, E. J., Hokke, C. H., Haas, H., Smits, H. H., & Yazdanbakhsh, M.
- Affiliations
- Washington University in St. Louis (US)
- Leiden University Medical Center (NL)
- Research Center Borstel - Leibniz Lung Center (DE)
- Department of Parasitology, Leiden University Medical Center, 2333 ZA Leiden, Netherlands 1
- University of Bonn (DE)
- Trudeau Institute (US)
- Corresponding author
- Yazdanbakhsh, Maria
- ORCID
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2012-09-10
- Volume
- 209
- Issue
- 10
- Pages
- 1753-1767
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC3457738
- OpenAlex
- W2158574746
- Cited by
- 236
- References
- 2
- Citations by year
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- FWCI
- 17.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion, cc-by-nc-sa)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Leiden Repository (Leiden University) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (700.55.013)
- National Institute of Allergy and Infectious Diseases (R01AI053825, AI53825)
- Topics
- Life Sciences › Immunology and Microbiology › Parasitology › Parasites and Host Interactions
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Health Sciences › Medicine › Infectious Diseases › Parasitic Diseases Research and Treatment
- Keywords
- omega_1, Schistosoma mansoni, Th2 polarization, dendritic cells, CD206, ribonuclease, glycosylation, soluble egg antigen, protein synthesis inhibition, mRNA degradation, ribosomal RNA degradation
- MeSH terms
- Mannose Receptor, Amino Acid Sequence, Animals, Cell Line, Cells, Cultured, Dendritic Cells, Endoribonucleases, Glycosylation, Humans, Molecular Sequence Data, Ovum, Receptors, Cell Surface, RNA, Messenger, RNA, Ribosomal, Schistosoma mansoni, Protein Biosynthesis, Th2 Cells, Lectins, C-Type, Mannose-Binding Lectins, Mice
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