Abstract
THE glycoprotein CD5 is expressed on the surface membrane of all mature T cells1 and a small proportion of B lymphocytes1,2. Its exact role in immune interactions is still unknown. Studies3–10indicate that CD5 functions both in mice and humans as a receptor, delivering co-stimulatory signals to T cells in a manner similar to CD2 (ref. 11) and CD28 (ref. 12). Anti-CDS antibodies stimulate both T-cell proliferation mediated by CD3 in association with the T-cell receptor and secretion of interleukin-2 and expression of its receptor, as well as inducing an increase in intracellular Ca2+concentration (refs 5–10). To identify the ligand for CD5 we purified the human CD5 protein, labelled it with biotin and used it as a probe. Here we report that CD5 specifically interacts with the cell-surface protein CD72 exclusive to B cells. This interaction is blocked by anti-CD72 antibodies, but not by any other anti-B-cell antibodies. Moreover, non-B cells (mouse L-cell fibroblasts and human Jurkat T cells) expressing a transfected human CD72 complementary DNA could bind to the CD5–biotin conjugate. The results demonstrate that the B-cell surface protein CD72 (Lyb-2 in mice) is the ligand for CD5.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Wang, C. Y., Good, R. A., Ammizate, P., Dymbert, G. & Evans, R. J. exp. Med. 151, 1539–1544 (1980).
Hayakawa, K. & Hardy, R. R. A. Rev. Immun. 6, 197–218 (1988).
Jones, N. H. et al. Nature 323, 346–349 (1986).
Huang, H. S., Jones, N. H., Strominger, J. L. & Herzenberg, L. A. Proc. natn. Acad. Sci. U.S.A. 84, 204–208 (1987).
Ceuppens, J. L. & Baroja, M. L. J. Immun. 137, 1816–1821 (1986).
Ledbetter, J. A., June, C. H., Grosmaire, L. S. & Rabinovitch, P. S. Proc. natn. Acad. Sci. U.S.A. 84, 1384–1388 (1987).
Nishimura, Y. et al. Eur. J. Immun. 18, 747–753 (1988).
Verwilghen, J., Vandesande, R., Vandenberghe, P. & Ceuppens, J. L. Cell. Immun. 131, 109–119 (1990).
Spertini, F., Stohl, W., Ramesh, N. Moody, C. & Geha, R. S. J. Immun. 146, 47–52 (1991).
Vandenberghe, P. & Ceupppens, J. L. Eur. J. Immun. 21, 251–259 (1991).
Springer, T. A. Nature 346, 425–434 (1990).
Linsley, P. S., Clark, E. A. & Ledbetter, J. A. Proc. natn. Acad. Sci. U.S.A. 87, 5031–5035 (1990).
Kürzinger, K. & Springer, T. A. J. biol. Chem. 257, 12412–12418 (1982).
Martin, S. D. & Springer, T. A. Cell 51, 813–819 (1987).
Taki, S., Shimamura, T., Abe, M., Shirai, T. & Takahora, Y. J. immunol. Meth. 122, 33–41 (1989).
McMichael, A. J. & Gotch, F. M. in Leucocyte Typing III (ed. McMichael, A. J.) 31–62 (Oxford University Press, Oxford, 1987).
Dörken, B., Möller, P., Pezzutto, A., Schwartz-Albiez, R. & Moldenhauer, G. in Leucocyte Typing IV (eds Knapp, W. et al.) 15–32 (Oxford University Press, Oxford, 1989).
Von Hoegen, I., Nakayama, E. & Parnes, J. R. J. Immun. 144, 4870–4877 (1990).
Von Hoegen, I., Hsieh, C., Schwarting, R. Francke, U. & Parnes, J. R. Eur. J. Immun. (in the press).
Schwarting, R. & Stein, H. in Leucocyte Typing IV (eds Knapp, W. et al.) 100–102 (Oxford University Press, Oxford, 1989).
Dörken, B., Möller, P., Pezzutto, A., Schwartz-Albiez, R. & Moldenhauer, G. in Leucocyte Typing IV (eds Knapp, W. et al) 99–100 (Oxford University Press, Oxford, 1989).
Nakayama, E., von Hoegen, I. & Parnes, J. R. Proc. natn. Acad. Sci. U.S.A. 86, 1352–1356 (1989).
Pezzutto, A., Dörken, B., Valentine, M. A., Shu, G. L. & Clark, E. A. in Leucocyte Typing IV (eds Knapp, W. et al.) 178–182 (Oxford University Press, Oxford, 1989).
Kamal, M., Katira, A. & Gordon, J. Eur. J. Immun. (in the press).
Subbarao, B. & Mosier, D. E. J. Immun. 140, 2033–2037 (1983).
Subbarao, B. & Melchers, F. Curr. Topics microbiol. Immun. 113, 72–76 (1984).
Snow, E. C., Mond, J. J. & Subbarao, B. J. Immun. 137, 1793–1796 (1986).
Subbarao, B., Morris, J. & Baluyut, A. R. Cell. Immun. 112, 329–342 (1988).
Yakura, H., Shen, F.-W., Kaemer, M. & Boyse, E. A. J. exp. med. 153, 129–135 (1981).
Subbarao, B. & Mosier, D. E. Immunol. Rev. 69, 81–97 (1982).
Gunning, P., Leavitt, J., Muscat, G., Ng, S.-Y. & Kedes, L. Proc. natn. Acad. Sci. U.S.A. 84, 4831–4837 (1987).
Hardin, J. A. et al. Cell Immun. 126, 304–321 (1990).
Kawamura, N. et al. J. clin. Invest. 78, 1331–1338 (1986).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
de Velde, H., von Hoegen, I., Luo, W. et al. The B-cell surface protein CD72/Lyb-2 is the ligand for CDS. Nature 351, 662–665 (1991). https://doi.org/10.1038/351662a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/351662a0
This article is cited by
-
The role of semaphorins in immune responses and autoimmune rheumatic diseases
Nature Reviews Rheumatology (2018)
-
CD22 and CD72 are inhibitory receptors dominantly expressed in B lymphocytes and regulate systemic autoimmune diseases
Zeitschrift für Rheumatologie (2017)
-
CD22 und CD72 sind in B‑Lymphozyten dominant exprimierte inhibitorische Rezeptoren und regulieren systemische Autoimmunerkrankungen
Zeitschrift für Rheumatologie (2016)
-
B cells with immune-regulating function in transplantation
Nature Reviews Nephrology (2014)
-
Evolution of the CD163 family and its relationship to the bovine gamma delta T cell co-receptor WC1
BMC Evolutionary Biology (2010)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
