부산대학교 도서관

Complexes between GDI molecules and self or microbial glycolipids represent important immunogenic ligands for specific subsets of T cells. However, the function of one of the GDI family members, CDIe, has yet to be determined. Here, we show that the mycobacterial antigens hexamannosylated phosphatidyl-myo-inositols (PIM[sub 6]) stimulate CD1b-restricted T cells only after partial digestion of the oligomannose moiety by lysosomal a-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[sub 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. [ABSTRACT FROM AUTHOR]