Schistosome-derived omega-1 drives Th2 polarization by suppressing protein synthesis following internalization by the mannose receptor.
J Exp Med
; 209(10): 1753-67, S1, 2012 Sep 24.
Article
en En
| MEDLINE
| ID: mdl-22966004
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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Schistosoma mansoni
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Biosíntesis de Proteínas
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Receptores de Superficie Celular
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Células Th2
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Lectinas Tipo C
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Lectinas de Unión a Manosa
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Endorribonucleasas
Límite:
Animals
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Humans
Idioma:
En
Año:
2012
Tipo del documento:
Article