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.