期刊
EUROPEAN JOURNAL OF IMMUNOLOGY
卷 40, 期 4, 页码 1185-1191出版社
WILEY
DOI: 10.1002/eji.200939936
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类别
资金
- Chinese National Natural Science Foundation [30730050, 30621063]
- Chinese State Key Program in Basic Research [2006CB910800, 2009CB522506, 2010CB911900]
- Chinese National High-tech Program [2009ZX09103-631, 2009ZX09503-002]
- State Key Laboratory of Proteomics [SKLP-Y200806]
LSECtin, a novel member of the C-type lectin DC-SIGN family, not only acts as an attachment factor for pathogens, but also recognizes endogenous activated T cells. The endogenous ligands of LSECtin, however, have remained unclear. In this study, we identified CD44 on Jurkat T cells as a candidate ligand of LSECtin, and confirmed the specific interaction between LSECtin and CD44. Moreover, we showed that LSECtin selectively bound CD44s, CD44v4 and CD44v8-10 by screening a series of typical CD44 isoforms. By deletion of the carbohydrate-recognition domain region and mutation of crucial amino acids involved in carbohydrate-recognition of LSECtin and by inhibition of the N-linked glycosylation of CD44, we further demonstrated that the interaction between CD44 and LSECtin is dependent on protein-glycan recognition. Our findings indicate that CD44 is the first identified endogenous ligand of LSECtin, and similarly, that LSECtin is a novel ligand of CD44. These findings provide important new perspectives on the biology of both LSECtin and CD44 in the immune system.
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