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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Oct 1;90(19):8797–8801. doi: 10.1073/pnas.90.19.8797

Enhancement of peptide antigen presentation by a second peptide.

A I de Kroon 1, H M McConnell 1
PMCID: PMC47447  PMID: 8105466

Abstract

The influence of nonstimulatory "competitor" peptides on the binding of an antigenic peptide to a major histocompatibility complex (MHC) class II molecule was investigated. Using high-performance size-exclusion chromatography and fluorescein-labeled peptides, we show that the presence of the peptides dynorphin A-(1-13) and poly(L-lysine) results in enhancement rather than inhibition of the binding of hen egg lysozyme peptide-(107-116) [HEL-(107-116)] to the detergent-solubilized mouse class II molecule IEd. In parallel, dynorphin A-(1-13) and poly(L-lysine) were found to enhance the specific activation of an IEd-restricted T-cell hybridoma by HEL-(107-116). A molecular mechanism involving an intermediate two peptide-MHC class II protein complex is proposed to explain the enhancement of peptide binding to class II molecules by an irrelevant second peptide.

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Selected References

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