Acknowledgements This research was supported by grants CA52511 and AI40617 from the National Institutes of Health, a grant from the Medical Research of Canada (Laurent Brossay) and a grant from the Association pour la Recherche contre le Cancer (Nicolas Burdin). We would like to thank the other members of our laboratory and Drs. S. Cardell, K. Hayakawa, M. Bix, R. Locksley, M. Grusby and Y. Koezuka for valuable advice, help and support. This is manuscript no. 234 of the La Jolla Institute of Allergy and Immunology.
Antigen-presenting function of mouse CD 1: one molecule with two different kinds of antigenic ligands
Version of Record online: 28 APR 2006
Volume 163, Issue 1, pages 139–150, June 1998
How to Cite
Brossay, L., Burdin, N., Tangri, S. and Kronenbers, M. (1998), Antigen-presenting function of mouse CD 1: one molecule with two different kinds of antigenic ligands. Immunological Reviews, 163: 139–150. doi: 10.1111/j.1600-065X.1998.tb01193.x
- Issue online: 28 APR 2006
- Version of Record online: 28 APR 2006
Summary: Mouse CDl (mCDl) is an antigen-presenting molecule that is constitutively expressed by most bone marrow-derived cells. Peptides with a hydrophobic binding motif can bind to mCDl, and the peptide-CDl complex is recognized by CD8+ cytolytic T cells. In contrast, NK1.1+ T cells, which are CD8-, are autoreactive for mCD 1 molecules. This autore-activity, along with the ability of NK T cells to rapidly produce large amounts of cytokine, has led to the suggestion that these cells may be immunoregulatory We have shown that die mCD l -autoreactive T cells can distinguish between different cell types that express similar levels of mCDl, suggesting that mCDl -bound autologous ligands may be critical for T-cell stimulation. Consistent with this, some of these mCDl-restricted T cells can recognize the glycolipid a-galactosyiceramide presented by mCDl, while others do not respond. The mCDl crystal structure reveals a deep and narrow hydrophobic antigen-binding site which can more easily bind lipid antigens than the long hydrophobic peptides that we have defined as mCDl antigens. The ability of mCDl to bind and present two different types of ligands raises the question as to how mCDl can accommodate both types of antigens.