Abstract
MAJOR histocompatibility complex (MHC) class I and class II molecules bind immunogenic peptides and present them to lymphocytes bearing the αβ T-cell antigen receptor (TCR)1-4. An analogous antigen-presenting function also has been proposed for the non-MHC-encoded GDI molecules5, a family of non-polymorphic, β2-microglobulin-associated glycoproteins5-8 expressed on most professional antigen-presenting cells9-11. In support of this hypothesis, CD1 molecules are recognized by selected CD4-CD8- αβ or γδ8TCR+ T-cell clones12-14, and we have recently shown that GDI molecules restrict the recognition of foreign microbial antigens by αβTGR+ T cells10. But the substantial structural divergence of GDI from MHC class I and class II molecules7, raises the possibility that the antigens presented by the GDI system may differ fundamentally from those presented by MHC-encoded molecules. Here we report that a purified CDlb-restricted antigen of Mycobacterium tuberculosis presented to αβTCR+ T cells is mycolic acid, a family of α-branched, β-hydroxy, long-chain fatty acids found in mycobacteria15,16. This example of non-protein microbial antigen recognition suggests that αβTCR+ T cells recognize a broader range of antigens than previously appreciated and that at least one member of the GDI family has evolved the ability to present lipid antigens.
Original language | English (US) |
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Pages (from-to) | 691-694 |
Number of pages | 4 |
Journal | Nature |
Volume | 372 |
Issue number | 6507 |
DOIs | |
State | Published - 1994 |
Externally published | Yes |
ASJC Scopus subject areas
- General