Role of Phosphatidylinositol Mannosides in the Interaction between Mycobacteria and DC-SIGN

N.N. Driessen, R. Ummels, J.J. Maaskant, S.S. Gurcha, G.S. Besra, G.D. Ainge, D.S. Larsen, G.F. Painter, C.M.J.E. Vandenbroucke-Grauls, J.J.G. Geurtsen, B.J. Appelmelk

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Abstract

The C-type lectin dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) is the major receptor on DCs for mycobacteria of the Mycobacterium tuberculosis complex. Recently, we have shown that although the mannose caps of the mycobacterial surface glycolipid lipoarabinomannan (ManLAM) are essential for the binding to DC-SIGN, genetic removal of these caps did not diminish the interaction of whole mycobacteria with DC-SIGN and DCs. Here we investigated the role of the structurally related glycolipids phosphatidylinositol mannosides (PIMs) as possible ligands for DC-SIGN. In a binding assay with both synthetic and natural PIMs, DC-SIGN exhibited a high affinity for hexamannosylated PIM
Original languageEnglish
Pages (from-to)4538-4547
JournalInfection and Immunity
Volume77
Issue number10
DOIs
Publication statusPublished - 2009

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