Biologic significance and therapeutic implications of antigen/MHC interactions.
Synthetic analog peptides of chicken ovalbumin have been synthesized that have up to a 10-fold higher capacity to bind a particular MHC specificity (IAd) than the natural peptide. Some of these peptides were very efficient in inhibiting induction of both in vitro and in vivo immune responses. However, factors other than the ability to bind to MHC are also important in defining the capacity of a particular peptide to function in vivo. The finding that the antigen-presenting functions of MHC can be inhibited in vivo opens up the possibility of using this as a therapeutic approach to MHC-associated autoimmune diseases.
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Cytel, La Jolla, California 92037.
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Lamont
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D000595:Amino Acid Sequence; D000818:Animals; D000938:Antigen-Presenting Cells / Q000276:immunology*; D001667:Binding, Competitive; D000939:Epitopes; D000949:Histocompatibility Antigens Class II / Q000276:immunology*; D007111:Immunity, Cellular; D066298:In Vitro Techniques; D008285:Major Histocompatibility Complex; D051379:Mice; D008969:Molecular Sequence Data; D010047:Ovalbumin / Q000276:immunology*; D010446:Peptide Fragments / Q000276:immunology; D013329:Structure-Activity Relationship
D000939:Epitopes; D000949:Histocompatibility Antigens Class II; D010446:Peptide Fragments; D010047:Ovalbumin