Assistance of Microbial Glycolipid Antigen Processing by CD1e

Author:

de la Salle Henri12345,Mariotti Sabrina12345,Angenieux Catherine12345,Gilleron Martine12345,Garcia-Alles Luis-Fernando12345,Malm Dag12345,Berg Thomas12345,Paoletti Samantha12345,Maître Blandine12345,Mourey Lionel12345,Salamero Jean12345,Cazenave Jean Pierre12345,Hanau Daniel12345,Mori Lucia12345,Puzo Germain12345,De Libero Gennaro12345

Affiliation:

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

2. Experimental Immunology, Department of Research, Basel University Hospital, CH-4031 Basel, Switzerland.

3. CNRS, UMR 5089, Immunochimie et Glycoconjugués Mycobacteriens, Institut de Pharmacologie et de Biologie Structurale, F-31077 Toulouse Cedex, France.

4. Biophysique Structurale, Département Mécanismes Moléculaires des Infections Mycobactériennes, Institut de Pharmacologie et de Biologie Structurale, F-31077 Toulouse Cedex, France.

5. Department of Medicine, University Hospital of Northern Norway, N-9038 Tromsø, Norway.

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 (PIM 6 ) stimulate CD1b-restricted T cells only after partial digestion of the oligomannose moiety by lysosomal α-mannosidase and that soluble CD1e is required for this processing. Furthermore, recombinant CD1e was able to bind glycolipids and assist in the digestion of PIM 6 . We propose that, through this form of glycolipid editing, CD1e helps expand the repertoire of glycolipidic T cell antigens to optimize antimicrobial immune responses.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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