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

By 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 and B.J. Appelmelk


2)-linked mannosyl residues identical to the mannose cap on ManLAM, but not for di- and tetramannosylated PIM2 and PIM4, respectively. To determine the role of PIM6 in the binding of whole mycobacteria to DC-SIGN, a mutant strain of M. bovis bacillus Calmette-Guerin deficient in the production of PIM6 (Delta pimE) was created, as well as a double knockout deficient in the production of both PIM6 and the mannose caps on LAM (Delta pimE Delta capA). Compared to the wild-type strain, both mutant strains bound similarly well to DC-SIGN and DCs. Furthermore, the wild-type and mutant strains induced comparable levels of interleukin-10 and interleukin-12p40 when used to stimulate DCs. Hence, we conclude that, like ManLAM, PIM6 represents a bona fide DC-SIGN ligand but that other, as-yet-unknown, ligands dominate in the interaction between mycobacteria and DC

Year: 2009
DOI identifier: 10.1128/IAI.01256-08
OAI identifier:
Provided by: DSpace at VU

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