Assistance of microbial glycolipid antigen processing by CD1e

Science. 2005 Nov 25;310(5752):1321-4. doi: 10.1126/science.1115301.

Henri de la Salle ¹, Sabrina Mariotti, Catherine Angenieux, Martine Gilleron, Luis-Fernando Garcia-Alles, Dag Malm, Thomas Berg, Samantha Paoletti, Blandine Maître, Lionel Mourey, Jean Salamero, Jean Pierre Cazenave, Daniel Hanau, Lucia Mori, Germain Puzo, Gennaro De Libero

Affiliations

Affiliation

1 INSERM, U725, Etablissement Francais du Sang-Alsace, F-67065 Strasbourg, France.

PMID: 16311334 DOI: 10.1126/science.1115301

Abstract

Complexes between CD1 molecules and self or microbial glycolipids represent important immunogenic ligands for specific subsets of T cells. However, the function of one of the CD1 family members, CD1e, has yet to be determined. Here, we show that the mycobacterial antigens hexamannosylated phosphatidyl-myo-inositols (PIM6) stimulate CD1b-restricted T cells only after partial digestion of the oligomannose moiety by lysosomal alpha-mannosidase and that soluble CD1e is required for this processing. Furthermore, recombinant CD1e was able to bind glycolipids and assist in the digestion of PIM6. We propose that, through this form of glycolipid editing, CD1e helps expand the repertoire of glycolipidic T cell antigens to optimize antimicrobial immune responses.

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