Identification of the mycobacterial carbohydrate structure that binds the C-type lectins DC-SIGN, L-SIGN and SIGNR1.
作者： Estella A. Koppel , Irene S. Ludwig , Marta Sanchez Hernandez , Todd L. Lowary , Rajendrakumar R. Gadikota
DOI: 10.1016/J.IMBIO.2004.03.003
关键词:
摘要: Mycobacterium tuberculosis represents a worldwide health risk and although macrophages are primarily infected, dendritic cells (DC) important in inducing cellular immune responses against M. tuberculosis. Recent studies have demonstrated that targets the DC-specific C-type lectin DC-SIGN to inhibit immuno-stimulatory function of DC through interaction mycobacterial mannosylated lipoarabinomannan (ManLAM) DC-SIGN, which prevents maturation induces immuno-suppressive cytokine IL-10. This may contribute survival persistence Here, we identified specific pathogen-derived carbohydrate structure on ManLAM is recognized by DC-SIGN. We synthesized mannose-cap oligosaccharides man-ara, (man)2-ara (man)3-ara, demonstrate these neoglycoconjugates specifically bound Moreover, human murine homologue L-SIGN SIGNR1, respectively, also interact with mycobacteria ManLAM. Both homologues highest affinity for (man)3-ara structure, similar study provides information about structures pathogens provide strategies develop vaccines pathogens. identification SIGNR1 as receptor will enable vivo investigate role pathogenesis.
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