The role of glycosylation in protein antigenic properties |
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Authors: | E Lisowska |
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Institution: | (1) Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Rudolf Weigl Street 12, 53-114 Wrocław (Poland), Fax + 48 71 373 2587, e-mail: lisowska@iitd.pan.wroc.pl., PL |
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Abstract: | Glycosylation of proteins is a common event and contributes to protein antigenic properties. Most data have been obtained
from model studies on glycoprotens with well-defined structure or synthetic glycopeptides and their respective monoclonal
antibodies. Antibodies raised against glycoprotein antigens may be specific for their carbohydrate units which are recognized
irrespective of the protein carrier (carbohydrate epitopes), or in the context of the adjacent amino acid residues (glycopeptidic
epitopes). Conformation or proper exposure of peptidic epitopes of glycoproteins is also frequently modulated by glycosylation
due to intramolecular carbohydrate-protein interactions. The effects of glycosylation are broad: glycosylation may 'inactivate'
the peptidic epitope or may be required for its reactivity with the antibody, depending on the structure of the antigenic
site and antibody fine specificity. Evidence is increasing that similar effects of glycosylation pertain to T cell-dependent
cellular immune responses. Glycosylated peptides can be bound and presented by MHC class I or II molecules and elicit glycopeptide-specific
T cell clones.
Received 5 July 2001; received after revision 9 October 2001; accepted 11 October 2001 |
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Keywords: | , Antibody, epitope, glycoprotein, glycosylation, MHC complex, N-glycan, O-glycan, Pepscan analysis, peptide, T cell,,,,,response, |
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