Altered glycosylation of recombinant NKp30 hampers binding to heparan sulfate: a lesson for the use of recombinant immunoreceptors as an immunological tool
Identifieur interne : 002C08 ( Main/Exploration ); précédent : 002C07; suivant : 002C09Altered glycosylation of recombinant NKp30 hampers binding to heparan sulfate: a lesson for the use of recombinant immunoreceptors as an immunological tool
Auteurs : Oren Hershkovitz ; Mostafa Jarahian [Israël] ; Alon Zilka ; Ahuva Bar-Ilan ; Guy Landau ; Sergey Jivov ; Yoram Tekoah ; Rachel Glicklis ; John T. Gallagher [Allemagne] ; Sabrina C. Hoffmann [Royaume-Uni] ; Hagit Zer ; Ofer Mandelboim [Israël] ; Carsten Watzl [Royaume-Uni] ; Frank Momburg [Israël] ; Angel Porgador [Israël]Source :
- Glycobiology [ 0959-6658 ] ; 2008.
Abstract
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 coligand 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 (Warren HS, Jones AL, Freeman C, Bettadapura J, Parish CR. 2005. Evidence that the cellular ligand for the human NK cell activation receptor NKp30 is not a heparan sulfate glycosaminoglycan. J Immunol. 175:207–212) 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 coligand for NKp30. At the cellular level, soluble heparan sulfate enhanced the secretion of IFNγ 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.
Url:
DOI: 10.1093/glycob/cwm125
Affiliations:
- Allemagne, Israël, Royaume-Uni
- Angleterre, Bade-Wurtemberg, District de Karlsruhe, Grand Manchester
- Heidelberg, Manchester
- Université de Manchester
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Gallagher</name><affiliation wicri:level="3"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Immunology, University of Heidelberg, Im Neuenheimer Feld 305, 69120 Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Hoffmann, Sabrina C" sort="Hoffmann, Sabrina C" uniqKey="Hoffmann S" first="Sabrina C." last="Hoffmann">Sabrina C. Hoffmann</name><affiliation wicri:level="4"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Medical Oncology, University of Manchester, Cancer Research UK, Christie, Hospital NHS Trust, Manchester M204BX</wicri:regionArea><orgName type="university">Université de Manchester</orgName><placeName><settlement type="city">Manchester</settlement><region type="nation">Angleterre</region><region nuts="2" type="region">Grand Manchester</region></placeName></affiliation></author><author><name sortKey="Zer, Hagit" sort="Zer, Hagit" uniqKey="Zer H" first="Hagit" last="Zer">Hagit Zer</name><affiliation><wicri:noCountry code="subField">Sciences</wicri:noCountry></affiliation></author><author><name sortKey="Mandelboim, Ofer" sort="Mandelboim, Ofer" uniqKey="Mandelboim O" first="Ofer" last="Mandelboim">Ofer Mandelboim</name><affiliation wicri:level="1"><country xml:lang="fr">Israël</country><wicri:regionArea>The Lautenberg Center for General and Tumor Immuno- logy, Hebrew University—Hadassah Medical School, Jerusalem</wicri:regionArea><wicri:noRegion>Jerusalem</wicri:noRegion></affiliation></author><author><name sortKey="Watzl, Carsten" sort="Watzl, Carsten" uniqKey="Watzl C" first="Carsten" last="Watzl">Carsten Watzl</name><affiliation wicri:level="4"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Medical Oncology, University of Manchester, Cancer Research UK, Christie, Hospital NHS Trust, Manchester M204BX</wicri:regionArea><orgName type="university">Université de Manchester</orgName><placeName><settlement type="city">Manchester</settlement><region type="nation">Angleterre</region><region nuts="2" type="region">Grand Manchester</region></placeName></affiliation></author><author><name sortKey="Momburg, Frank" sort="Momburg, Frank" uniqKey="Momburg F" first="Frank" last="Momburg">Frank Momburg</name><affiliation wicri:level="1"><country xml:lang="fr">Israël</country><wicri:regionArea>Center for Glycobiology, Department of Biotechnology Engineering, Ben-Gurion University of the Negev, Beer-Sheva, 84105</wicri:regionArea><wicri:noRegion>84105</wicri:noRegion></affiliation></author><author><name sortKey="Porgador, Angel" sort="Porgador, Angel" uniqKey="Porgador A" first="Angel" last="Porgador">Angel Porgador</name><affiliation></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Israël</country></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Israël</country></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Glycobiology</title><idno type="ISSN">0959-6658</idno><idno type="eISSN">1460-2423</idno><imprint><publisher>Oxford University Press</publisher><date type="published">2008</date><date type="e-published">2007</date><biblScope unit="vol">18</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="28">28</biblScope><biblScope unit="page" to="41">41</biblScope></imprint><idno type="ISSN">0959-6658</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0959-6658</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">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 coligand 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 (Warren HS, Jones AL, Freeman C, Bettadapura J, Parish CR. 2005. Evidence that the cellular ligand for the human NK cell activation receptor NKp30 is not a heparan sulfate glycosaminoglycan. J Immunol. 175:207–212) 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 coligand for NKp30. At the cellular level, soluble heparan sulfate enhanced the secretion of IFNγ 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.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Israël</li><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Bade-Wurtemberg</li><li>District de Karlsruhe</li><li>Grand Manchester</li></region><settlement><li>Heidelberg</li><li>Manchester</li></settlement><orgName><li>Université de Manchester</li></orgName></list><tree><noCountry><name sortKey="Bar Ilan, Ahuva" sort="Bar Ilan, Ahuva" uniqKey="Bar Ilan A" first="Ahuva" last="Bar-Ilan">Ahuva Bar-Ilan</name><name sortKey="Glicklis, Rachel" sort="Glicklis, Rachel" uniqKey="Glicklis R" first="Rachel" last="Glicklis">Rachel Glicklis</name><name sortKey="Hershkovitz, Oren" sort="Hershkovitz, Oren" uniqKey="Hershkovitz O" first="Oren" last="Hershkovitz">Oren Hershkovitz</name><name sortKey="Jivov, Sergey" sort="Jivov, Sergey" uniqKey="Jivov S" first="Sergey" last="Jivov">Sergey Jivov</name><name sortKey="Landau, Guy" sort="Landau, Guy" uniqKey="Landau G" first="Guy" last="Landau">Guy Landau</name><name sortKey="Tekoah, Yoram" sort="Tekoah, Yoram" uniqKey="Tekoah Y" first="Yoram" last="Tekoah">Yoram Tekoah</name><name sortKey="Zer, Hagit" sort="Zer, Hagit" uniqKey="Zer H" first="Hagit" last="Zer">Hagit Zer</name><name sortKey="Zilka, Alon" sort="Zilka, Alon" uniqKey="Zilka A" first="Alon" last="Zilka">Alon Zilka</name></noCountry><country name="Israël"><noRegion><name sortKey="Jarahian, Mostafa" sort="Jarahian, Mostafa" uniqKey="Jarahian M" first="Mostafa" last="Jarahian">Mostafa Jarahian</name></noRegion><name sortKey="Mandelboim, Ofer" sort="Mandelboim, Ofer" uniqKey="Mandelboim O" first="Ofer" last="Mandelboim">Ofer Mandelboim</name><name sortKey="Momburg, Frank" sort="Momburg, Frank" uniqKey="Momburg F" first="Frank" last="Momburg">Frank Momburg</name><name sortKey="Porgador, Angel" sort="Porgador, Angel" uniqKey="Porgador A" first="Angel" last="Porgador">Angel Porgador</name><name sortKey="Porgador, Angel" sort="Porgador, Angel" uniqKey="Porgador A" first="Angel" last="Porgador">Angel Porgador</name></country><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Gallagher, John T" sort="Gallagher, John T" uniqKey="Gallagher J" first="John T." last="Gallagher">John T. Gallagher</name></region></country><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Hoffmann, Sabrina C" sort="Hoffmann, Sabrina C" uniqKey="Hoffmann S" first="Sabrina C." last="Hoffmann">Sabrina C. Hoffmann</name></region><name sortKey="Watzl, Carsten" sort="Watzl, Carsten" uniqKey="Watzl C" first="Carsten" last="Watzl">Carsten Watzl</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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