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Glycobiology Advance Access published online on June 9, 2004
Glycobiology, doi:10.1093/glycob/cwh109
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Received February 28, 2004
Revised June 3, 2004
Accepted June 4, 2004

ORIGINAL ARTICLES

The mannose receptor fails to enhance processing and presentation of a glycoprotein antigen in transfected fibroblasts

Catherine E. Napper 1 Maureen E. Taylor 1*

1 Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK

* To whom correspondence should be addressed. E-mail: mt{at}glycob.ox.ac.


  Abstract

One function proposed for the mannose receptor, which is found on dendritic cells as well as on macrophages and hepatic endothelial cells, is in enhancing uptake and processing of glycoprotein antigens for presentation by MHC class II molecules. In this study, a direct assessment of the possible role of the mannose receptor in this process was made in the absence of other endocytic receptors that can internalize glycoproteins. Presentation of ribonuclease A and B peptides was compared in transfected fibroblasts co-expressing the mannose receptor and MHC class II molecules. Ribonuclease B bears a high mannose oligosaccharide and is a ligand for the mannose receptor whereas ribonuclease A is not glycosylated and is taken up by pinocytosis. Incubation of ribonucleases A or B with the transfected cells resulted in identical stimulation of ribonuclease-specific T cells, indicating that endocytosis of the glycosylated protein by the mannose receptor does not enhance presentation of this antigen. The postulated role of the mannose receptor in presentation of glycoprotein-derived antigen is re-evaluated in the light of these results.

Key words: Mannose receptor, endocytosis, antigen presentation, MHC class II


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