Polyisoprenyl glycolipids as targets of CD1-mediated T cell responses |
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Authors: | DB Moody |
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Institution: | (1) Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School, Smith Building Room 514, 1 Jimmy Fund Way, Boston, Massachusetts 02115 (USA), Fax +1 617 525 1010, e-mail: bmoody@rics.bwh.harvard.edu, US |
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Abstract: | T cells are well known to recognize peptide antigens presented by major histocompatibility (MHC) class I or class II molecules.
More recently, the CD1 family of antigen-presenting molecules has been shown to present both mammalian and microbial glycolipid
antigens for specific recognition by T cells. Human CD1c proteins mediate T cell recognition of polyisoprenyl glycolipids,
evolutionarily conserved phosphoglycolipids, which function in glycan synthesis pathways. This family of antigenic molecules
is particularly attractive for the study of the molecular features that control T cell recognition of self and foreign glycolipids
because natural polyisoprenols from mammals, fungi, protozoa, mycobacteria and eubacteria differ in structure. Moreover, these
naturally occurring structural differences can influence their recognition by CD1c-restricted T cells. This review of the
structural diversity and evolutionary relationships of polyisoprenoid glycolipids emphasizes those features of polyisoprenyl
glycolipid biosynthesis that are relevant to their functions as targets of CD1-mediated T cell responses.
Received 16 March 2001; received after revision 19 April 2001; accepted 23 April 2001 |
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Keywords: | , Polyisoprenol, dolichol, antigen presentation, CD1, T cell, mycobacteria, N-linked glycosylation, |
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