Skip Navigation


Glycobiology Advance Access originally published online on June 9, 2004
Glycobiology 2004 14(10):7C-12C; doi:10.1093/glycob/cwh109
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
14/10/7C    most recent
cwh109v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Napper, C. E.
Right arrow Articles by Taylor, M. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Napper, C. E.
Right arrow Articles by Taylor, M. E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology vol. 14 no. 10 © Oxford University Press 2004; all rights reserved.

COMMUNICATION

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

Catherine E. Napper and Maureen E. Taylor1

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

Received on February 28, 2004; revised on June 3, 2004; accepted on June 4, 2004

One function proposed for the mannose receptor 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 major histocompatibility complex (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 RNase A and B peptides was compared in transfected fibroblasts coexpressing the mannose receptor and MHC class II molecules. RNase B bears a high-mannose oligosaccharide and is a ligand for the mannose receptor, whereas RNase A is not glycosylated and is taken up by pinocytosis. Incubation of RNase 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 reevaluated in light of these results.

1 To whom correspondence should be addressed; e-mail: mt{at}glycob.ox.ac


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Immunol.Home page
L.-Z. He, A. Crocker, J. Lee, J. Mendoza-Ramirez, X.-T. Wang, L. A. Vitale, T. O'Neill, C. Petromilli, H.-F. Zhang, J. Lopez, et al.
Antigenic Targeting of the Human Mannose Receptor Induces Tumor Immunity
J. Immunol., May 15, 2007; 178(10): 6259 - 6267.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
E. J. McKenzie, P. R. Taylor, R. J. Stillion, A. D. Lucas, J. Harris, S. Gordon, and L. Martinez-Pomares
Mannose Receptor Expression and Function Define a New Population of Murine Dendritic Cells
J. Immunol., April 15, 2007; 178(8): 4975 - 4983.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.