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Lookup NU author(s): Dr Alexei von Delwig, Dr Julie Musson, Dr Norman Balfour-McKie, Dr Joseph Gray, Professor John Robinson
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We studied major histocompatibility complex class II-dependent presentation of two T cell epitopes delivered as synthetic peptides by fixed macrophages. Treatment of bone marrow macrophages with inhibitors of proteinases of the metallo-, aspartic and serine proteinase families enhanced presentation of peptides, indicating that several enzyme families participate in destructive antigen processing of exogenous peptides. High performance liquid chromatography and mass spectrometry analysis demonstrated the presence of peptide fragments in macrophage supernatants, and permitted identification of the cleavage sites which confirmed the enzyme families involved. Peptide fragments were shown to be competitive inhibitors of presentation of the full-length peptide to CD4 T cells by fixed and live macrophages. The results indicate that several classes of proteinases can modulate antigen presentation by at least two mechanisms: (1) degradation of extracellular oligopeptides and (2) generation of natural peptide ligands that block antigen presentation to CD4 T cells. The generation of inhibitory natural peptide ligands is a new mechanism of immunoregulation which could operate during the induction of T cell responses in a variety of situations.
Author(s): von Delwig A, Musson JA, Balfour-McKie N, Gray J, Robinson JH
Publication type: Article
Publication status: Published
Journal: European Journal of Immunology
Year: 2003
Volume: 33
Issue: 12
Pages: 3359-3366
Print publication date: 01/12/2003
ISSN (print): 0014-2980
ISSN (electronic): 1521-4141
Publisher: Wiley - VCH Verlag GmbH & Co. KGaA
URL: http://dx.doi.org/10.1002/eji.200324461
DOI: 10.1002/eji.200324461
PubMed id: 14635044
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