Said M Shawar, R&D Department, SA Scientific, San Antonio, Texas, USA

Copyright © 1998 Elsevier Ltd. All Rights Reserved.

The CD1 family of cell surface glycoproteins is a well-defined group of non-major histocompatibility complex (MHC) encoded molecules. This nonpoly-morphic cluster is the best understood of the MHC-unlinked antigen-presenting molecules. Five CD1 genes (CDla, b, c, d and e) have been identified in humans and two genes (mCDl.l and mCD1.2) in the mouse. However, CD1 genes and their products are evolutionarily conserved in mammals as they were identified in rats, rabbits, guinea pigs, cows and sheep.

Apparently, CD1 molecules represent a third and distinct lineage of antigen-presenting molecules that differ from MHC class I and class II molecules. Whereas CD1 molecules are structurally similar to MHC class I molecules and are associated with 02-microglobulin ((32m), their expression at the cell surface requires an endocytic compartment similar to MHC class II molecules.

CDla was fortuitously discovered in 1979 as the first human leukocyte antigen (HLA) recognized by a monoclonal antibody. Nevertheless, the most remarkable discovery regarding these molecules was reported only a few years ago when human CD lb was shown to present a nonpeptide antigen to T cells. Indeed, CD1 proteins are capable of presenting nonpeptide antigens such as microbial lipids and gly-colipids as well as peptide antigens. Such novel bio chemical properties may reflect a specialized role for CD1 in the immune system and the potential to exploit it in vaccine development.

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