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Glycobiology Advance Access published online on November 15, 2007
Glycobiology, doi:10.1093/glycob/cwm125
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Altered Glycosylation of Recombinant NKp30 Hampers Binding to Heparan Sulfate: a Lesson for the Use of Recombinant Immuno-Receptors as an Immunological Tool

Oren Hershkovitz*, Mostafa Jarahian{dagger}, Alon Zilka*, Ahuva Bar-Ilan*, Guy Landau*, Sergey Jivov*, Yoram Tekoah{ddagger}, Rachel Glicklis{ddagger}, John T. Gallagher{euro}, Sabrina C. Hoffmann§, Hagit Zer, Ofer Mandelboim#, Carsten Watzl§, Frank Momburg{dagger} and Angel Porgador*

* The Shraga Segal Department of Microbiology and Immunology, Faculty of Health Sciences and the Cancer Research Center, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel
{dagger} Division of Molecular Immunology, German Cancer Research Center, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany
{ddagger} Center for Glycobiology, Department of Biotechnology Engineering, Ben-Gurion University of the Negev, Beer-Sheva, 84105, Israel
{euro} Department of Medical Oncology, University of Manchester, Cancer Research UK, Christie, Hospital NHS Trust, Manchester M204BX, United Kingdom
§ Institute for Immunology, University of Heidelberg, Im Neuenheimer Feld 305, 69120 Heidelberg, Germany
Biacore Laboratory, Interdepartmental Equipment Unit, Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, Israel
# The Lautenberg Center for General and Tumor Immunology, Hebrew University – Hadassah Medical School, Jerusalem, Israel

Corresponding author Angel Porgador, Ph.D., Department of Microbiology and Immunology, Faculty of Health Sciences, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel Tel: 972-8-647-7283, Fax: 972-8-647-2574, e-mail: angel{at}bgu.ac.il

Received on April 4, 2007; accepted on November 5, 2007

NKp30 is a natural cytotoxicity receptor expressed by human NK cells and involved in NK lytic activity. We previously published that membranal heparan sulfate serves as a co-ligand for human NKp30. In the present study, we complement our results by showing direct binding of recombinant NKp30 to immobilized heparin. The heparan sulfate epitope(s) on target tumor cells and the heparin epitope(s) recognized by NKp30 share similar characteristics. Warren and colleagues (2005) published that NKp30 does not bind to membranal heparan sulfate on target cells and that heparan sulfate is not involved in NKp30-mediated lysis. In the current study, we examine the binding of six different recombinant NKp30s to membranal heparan sulfate and conclude that NKp30 does interact with membranal heparan sulfate. Yet, two of the six recombinant NKp30s, including the commercially available recombinant NKp30 (employed by Warren et al), did not show heparan sulfate-dependent binding. We demonstrate that this is due to an altered glycosylation of these two recombinant NKp30s. Upon removal of its N-linked glycans, heparan sulfate-dependent binding to tumor cells and direct binding to heparin were restored. Overall, our results emphasize the importance of proper glycosylation for analysis of NKp30 binding to its ligand and that membranal heparan sulfate could serve as a co-ligand for NKp30. At the cellular level, soluble heparan sulfate enhanced the secretion of IFN{gamma} by NK-92 natural killer cells activated with anti-NKp30 monoclonal antibody. We discuss the involvement of heparan sulfate binding to NKp30 in NKp30-mediated activation of NK cells.

Key words: Glycosylation / Heparan Sulfate / Natural Killer / NCR / NKp30


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