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The Journal of Immunology, Vol 157, Issue 8 3436-3442, Copyright © 1996 by American Association of Immunologists
ARTICLES |
A Bot, S Bot, S Antohi, K Karjalainen and C Bona
Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10029, USA. bot@msvax.mssm.edu
We had previously shown that a genetically engineered Ig expressing an immunodominant CD4+ T epitope corresponding to the 110-120 amino acids of influenza virus hemagglutinin (HA), activated T cells more efficiently than the synthetic peptide. Taking advantage of a T cell hybridoma specific for HA 110-120 and transfected with a reporter gene under the IL-2 promoter, we studied the kinetics of generation and persistence on surface MHC-II of the HA 110-120 peptide derived from various carriers. Our results show that the generation rate of immunogenic MHC II-peptide complex is dependent on the nature of the carrier. Abs specific for HA 110-120 peptide or for other epitopes on HA affect through various mechanisms the presentation of HA 110-120 peptide to T cells. The persistence of immunogenic MHC II-peptide complex on the surface of APC is not dependent on the nature of the carrier and correlates with the half-life of class II molecules, suggesting an irreversible binding of peptides to MHC-II molecules in 2PK3 murine B lymphoma cells.
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