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Glycobiology Advance Access published online on November 3, 2005
Glycobiology, doi:10.1093/glycob/cwj053
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received July 28, 2005
Revised October 2, 2005
Accepted October 27, 2005

Article

{alpha}2,6 Sialylation Promotes Binding of Placental Protein 14 via Its Ca2+ -Dependent Lectin Activity: Insights into Differential Effects on CD45RO and CD45RA T Cells

Eliran Ish-Shalom 1, Ari Gargir 2, Sabine André 3, Zipora Borovsky 1, Zohar Ochanuna 1, Hans-Joachim Gabius 3, Mark L. Tykocinski 4, and Jacob Rachmilewitz 1*

1 Goldyne Savad Institute of Gene Therapy, Hadassah-Hebrew University Medical Center, Jerusalem, Israel
2 Glycominds Ltd., Lod 71291, Israel
3 Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Vetarinärstr. 13, D-80539 Munich, Germany
4 Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA, 19104

* To whom correspondence should be addressed.
Jacob Rachmilewitz, E-mail: rjacob{at}md.huji.ac.il


  Abstract

Placental protein 14 (PP14; glycodelin) is a pregnancy-associated immunoregulatory protein that is known to inhibit T cells via T cell receptor desensitization. The recent demonstration of PP14 as lectin has provided insight into how it may mediate its CD45 glycoprotein-dependent T cell inhibition. In the present study, we have investigated PP14’s lectin binding properties in detail. Significantly, PP14 reacts with N-acetyllactosamine as was also found for members of the galectin family, such as the potent immunoregulatory protein, galectin-1. However, in contrast to galectin-1, PP14’s binding is significantly enhanced by {alpha}2,6-sialylation and also by the presence of cations. This was demonstrated by preferential binding to fetuin as compared to its desialylated variant asialofetuin, and by using free {alpha}2,6-vs {alpha}2,3-sialylated forms of N-acetyllactosamine in competitive inhibition and direct solid-phase binding assays. Interestingly, from immunological point of view, PP14 also binds differentially to CD45 isoforms known to differ in their degree of sialylation. PP14 preferentially inhibits CD45RA+, as compared to CD45RO+ T cells, and preferentially co-capped this variant CD45 on the T cell surface. Finally, we demonstrate that PP14 promotes CD45 dimerization and clustering, a phenomenon that may regulate CD45 activity.

Keywords: CD45/galectin/glycodelin/sialic acid/T cell.
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