Skip Navigation



International Immunology Advance Access published online on July 24, 2008
International Immunology, doi:10.1093/intimm/dxn081
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
20/10/1247    most recent
dxn081v1
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
Google Scholar
Right arrow Articles by Rossi, N. E.
Right arrow Articles by Regueiro, J. R.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rossi, N. E.
Right arrow Articles by Regueiro, J. R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Japanese Society for Immunology. 2008. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Differential antibody binding to the surface {alpha}βTCR·CD3 complex of CD4+ and CD8+ T lymphocytes is conserved in mammals and associated with differential glycosylation

Nineth E. Rossi1, Jesús Reiné1, Miguel Pineda-Lezamit2, Manuel Pulgar2, Néstor W. Meza3, Mahima Swamy4, Ruth Risueno2, Wolfgang W. A. Schamel4, Pedro Bonay2, Edgar Fernández-Malavé1,2 and José R. Regueiro1

1 Inmunología, Facultad de Medicina, Universidad Complutense, Madrid, Spain
2 Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Cantoblanco, Madrid, Spain
3 Centro de Investigaciones Energéticas, Medioambientales y Tecnológicas, Madrid, Spain
4 Department of Molecular Immunology, Max Planck-Institute for Immunobiology and Faculty of Biology, University of Freiburg, Freiburg, Germany

Correspondence to: Correspondence to: José R. Regueiro; E-mail: regueiro{at}med.ucm.es

We have previously shown that the surface {alpha}β T cell antigen receptor (TCR)·CD3 complex borne by human CD4+ and CD8+ T lymphocytes can be distinguished using mAbs. Using two unrelated sets of antibodies, we have now extended this finding to the surface {alpha}βTCR·CD3 of seven additional mammalian species (six non-human primates and the mouse). We have also produced data supporting that differential glycosylation of the two main T cell subsets is involved in the observed TCR·CD3 antibody-binding differences in humans. First, we show differential lectin binding to human CD4+ versus CD8+ T lymphocytes, particularly with galectin 7. Second, we show that certain lectins can compete differentially with CD3 mAb binding to human primary CD4+ and CD8+ T lymphocytes. Third, N-glycan disruption using swainsonine was shown to increase mAb binding to the {alpha}βTCR·CD3. We conclude that the differential antibody binding to the surface {alpha}βTCR·CD3 complex of primary CD4+ and CD8+ T lymphocytes is phylogenetically conserved and associated with differential glycosylation. The differences may be exploited for therapeutic purposes, such as T cell lineage-specific immunosuppression of graft rejection. Also, the impact of glycosylation on CD3 antibody binding requires a cautious interpretation of CD3 expression levels and T cell numbers in clinical diagnosis.

Keywords: cell surface molecules, T cells, TCRs

Transmitting editor: I. Pecht

Received 14 September 2007, accepted 26 June 2008.


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




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.