Abstract
Before their recognition by T lymphocytes, protein antigens gen-erally require processing by antigen-presenting cells1. In a poorly understood series of events, the protein antigen is internalized, transformed and re-expressed on the surface of the antigen-pres-enting cell in association with gene products of the major histocompatibility complex (MHC). Small peptides derived from the native protein can be recognized in the absence of antigen processing2–5, suggesting that processing involves proteolytic degradation. These peptides are thought to mimic the naturally produced peptide fragment. We describe here a synthetic peptide antigen of this type which does not require processing but which is nevertheless further processed by splenic antigen-presenting cells. Interestingly, this processing event specifically alters the interaction of the peptide with the class II MHC (la) molecule, markedly affecting both its potency as an antigen in vitro and its immunogenicity in vivo (IR gene control).
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Fox, B., Carbone, F., Germain, R. et al. Processing of a minimal antigenic peptide alters its interaction with MHC molecules. Nature 331, 538–540 (1988). https://doi.org/10.1038/331538a0
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DOI: https://doi.org/10.1038/331538a0
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