Toggle Main Menu Toggle Search

Open Access padlockePrints

Regulation of peptide presentation by major histocompatibility complex class II molecules at the surface of macrophages

Lookup NU author(s): Dr Alexei von Delwig, Dr Julie Musson, Dr Norman Balfour-McKie, Dr Joseph Gray, Professor John Robinson


Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


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.

Publication metadata

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


DOI: 10.1002/eji.200324461

PubMed id: 14635044


Altmetrics provided by Altmetric