The B7 homolog butyrophilin BTN2A1 is a novel ligand for DC-SIGN

被引:47
作者
Malcherek, Georg [1 ]
Mayr, Luzia [1 ]
Roda-Navarro, Pedro [1 ]
Rhodes, David [1 ]
Miller, Nigel [1 ]
Trowsdale, John [1 ]
机构
[1] Univ Cambridge, Dept Pathol, Div Immunol, Cambridge CB2 1QP, England
基金
英国医学研究理事会; 英国惠康基金;
关键词
D O I
10.4049/jimmunol.179.6.3804
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
The MHC-encoded butyrophilin, BTN2A1, is a cell surface glycoprotein related to the extended family of B7 costimulatory molecules. BTN2A1 mRNA was expressed in most human tissues, but protein expression was significantly lower in leukocytes. An Ig-fusion protein of BTN2A1 bound to immature monocyte-derived dendritic cells. Binding diminished upon MoDC maturation and no binding was detected to Langerhans cells. Induction of the counterreceptor was IL-4 dependent and occurred early during dendritic cell differentiation. The interaction required the presence of Ca2+ and was mediated by high-mannose oligosaccharides. These properties matched DC-SIGN, a DC-specific HIV-1 entry receptor. This was confirmed by binding of soluble BTN2A1 to DC-SIGN-transfectants and its inhibition by a specific Ab. DC-SIGN bound to native BTN2A1 expressed on a range of tissues. However, BTN2A1 was not recognized on some normal cells such as HUVECs despite a similar expression level. The BTN2A1 of tumor cells such as HEK293T have more high-mannose moieties in comparison to HUVECs, and those high-mannose moieties are instrumental for binding to DC-SIGN. The data are consistent with tumor- or tissue-specific glycosylation of BTN2A1 governing recognition by DC-SIGN on immature monocyte-derived dendritic cells.
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收藏
页码:3804 / 3811
页数:8
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