title: Assistance of microbial glycolipid antigen processing by CD1e.
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.
authors.affiliation: INSERM, U725, Etablissement Francais du Sang-Alsace, F-67065 Strasbourg, France.
authors.forename: Henri
authors.initials: H
authors.lastname: de la Salle
authors.forename: Sabrina
authors.initials: S
authors.lastname: Mariotti
authors.forename: Catherine
authors.initials: C
authors.lastname: Angenieux
authors.forename: Martine
authors.initials: M
authors.lastname: Gilleron
authors.forename: Luis-Fernando
authors.initials: LF
authors.lastname: Garcia-Alles
authors.forename: Dag
authors.initials: D
authors.lastname: Malm
authors.forename: Thomas
authors.initials: T
authors.lastname: Berg
authors.forename: Samantha
authors.initials: S
authors.lastname: Paoletti
authors.forename: Blandine
authors.initials: B
authors.lastname: Maître
authors.forename: Lionel
authors.initials: L
authors.lastname: Mourey
authors.forename: Jean
authors.initials: J
authors.lastname: Salamero
authors.forename: Jean Pierre
authors.initials: JP
authors.lastname: Cazenave
authors.forename: Daniel
authors.initials: D
authors.lastname: Hanau
authors.forename: Lucia
authors.initials: L
authors.lastname: Mori
authors.forename: Germain
authors.initials: G
authors.lastname: Puzo
authors.forename: Gennaro
authors.initials: G
authors.lastname: De Libero
mesh_terms: D000215:Acylation; D017951:Antigen Presentation; D000938:Antigen-Presenting Cells / Q000276:immunology; D000942:Antigens, Bacterial / Q000276:immunology* / Q000378:metabolism*; D018949:Antigens, CD1 / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D045744:Cell Line, Tumor; D003713:Dendritic Cells / Q000201:enzymology / Q000276:immunology; D006017:Glycolipids / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008213:Lymphocyte Activation; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000276:immunology; D010716:Phosphatidylinositols / Q000276:immunology* / Q000378:metabolism*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000276:immunology / Q000378:metabolism; D012995:Solubility; D013601:T-Lymphocytes / Q000276:immunology; D014162:Transfection; D043323:alpha-Mannosidase / Q000276:immunology
chemical_list: D000942:Antigens, Bacterial; D018949:Antigens, CD1; C419394:CD1b antigen; C417738:CD1e antigen; D006017:Glycolipids; D010716:Phosphatidylinositols; D011994:Recombinant Proteins; C034154:phosphatidylinositol mannoside; D043323:alpha-Mannosidase