Characterization of murine MGL1 and MGL2 C-type lectins: Distinct glycan specificities and tumor binding properties
Antigen presenting cells (APC) express a variety of pattern recognition receptors, including the C-type lectin receptors (CLR) that specifically recognize carbohydrate structures expressed on self-tissue and pathogens. The CLR play an important role in antigen uptake and presentation and have been s...
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| Veröffentlicht in: | Molecular immunology 2009-03, Vol.46 (6), p.1240-1249 |
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| creator | Singh, Satwinder Kaur Streng-Ouwehand, Ingeborg Litjens, Manja Weelij, Danny R. García-Vallejo, Juan Jesús van Vliet, Sandra J. Saeland, Eirikur van Kooyk, Yvette |
| description | Antigen presenting cells (APC) express a variety of pattern recognition receptors, including the C-type lectin receptors (CLR) that specifically recognize carbohydrate structures expressed on self-tissue and pathogens. The CLR play an important role in antigen uptake and presentation and have been shown to mediate cellular interactions. The ligand specificity of the human macrophage galactose-type lectin (MGL) has been characterized extensively. Here, we set out to determine the glycan specificity of the murine homologues, MGL1 and MGL2, using a glycan array. Murine MGL1 was found to be highly specific for Lewis X and Lewis A structures, whereas mMGL2, more similar to the human MGL, recognized N-actetylgalactosamine (GalNAc) and galactose, including the O-linked Tn-antigen, TF-antigen and core 2. The generation of MGL1 and MGL2-Fc proteins allowed us to identify ligands in lymph nodes, and MGL1-Fc additionally recognized high endothelial venules. Strikingly, MGL2 interacted strongly to adenocarcinoma cells, suggesting a potential role in tumor immunity. |
| doi_str_mv | 10.1016/j.molimm.2008.11.021 |
| format | Article |
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The CLR play an important role in antigen uptake and presentation and have been shown to mediate cellular interactions. The ligand specificity of the human macrophage galactose-type lectin (MGL) has been characterized extensively. Here, we set out to determine the glycan specificity of the murine homologues, MGL1 and MGL2, using a glycan array. Murine MGL1 was found to be highly specific for Lewis X and Lewis A structures, whereas mMGL2, more similar to the human MGL, recognized N-actetylgalactosamine (GalNAc) and galactose, including the O-linked Tn-antigen, TF-antigen and core 2. The generation of MGL1 and MGL2-Fc proteins allowed us to identify ligands in lymph nodes, and MGL1-Fc additionally recognized high endothelial venules. Strikingly, MGL2 interacted strongly to adenocarcinoma cells, suggesting a potential role in tumor immunity.</description><identifier>ISSN: 0161-5890</identifier><identifier>EISSN: 1872-9142</identifier><identifier>DOI: 10.1016/j.molimm.2008.11.021</identifier><identifier>PMID: 19162326</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Adenocarcinoma - metabolism ; Animals ; Antigen presenting cells ; Antigen-Presenting Cells - immunology ; Asialoglycoproteins - genetics ; Asialoglycoproteins - immunology ; Asialoglycoproteins - metabolism ; Bone Marrow Cells - metabolism ; C-type lectins ; Carbohydrate recognition ; Cell Line, Tumor ; Cells, Cultured ; Endothelium, Vascular - metabolism ; Extracellular Matrix - metabolism ; Lectins, C-Type - genetics ; Lectins, C-Type - immunology ; Lectins, C-Type - metabolism ; Ligands ; Lymph Nodes - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - immunology ; Membrane Proteins - metabolism ; MGL ; Mice ; Mice, Inbred C57BL ; Polysaccharides - metabolism ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Skin - metabolism</subject><ispartof>Molecular immunology, 2009-03, Vol.46 (6), p.1240-1249</ispartof><rights>2009</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-428d1c39bf27e3af8f2b14aaf154ce03f53b5f2f0ea91c57a31b8d2af03b6e313</citedby><cites>FETCH-LOGICAL-c426t-428d1c39bf27e3af8f2b14aaf154ce03f53b5f2f0ea91c57a31b8d2af03b6e313</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.molimm.2008.11.021$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19162326$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Singh, Satwinder Kaur</creatorcontrib><creatorcontrib>Streng-Ouwehand, Ingeborg</creatorcontrib><creatorcontrib>Litjens, Manja</creatorcontrib><creatorcontrib>Weelij, Danny R.</creatorcontrib><creatorcontrib>García-Vallejo, Juan Jesús</creatorcontrib><creatorcontrib>van Vliet, Sandra J.</creatorcontrib><creatorcontrib>Saeland, Eirikur</creatorcontrib><creatorcontrib>van Kooyk, Yvette</creatorcontrib><title>Characterization of murine MGL1 and MGL2 C-type lectins: Distinct glycan specificities and tumor binding properties</title><title>Molecular immunology</title><addtitle>Mol Immunol</addtitle><description>Antigen presenting cells (APC) express a variety of pattern recognition receptors, including the C-type lectin receptors (CLR) that specifically recognize carbohydrate structures expressed on self-tissue and pathogens. The CLR play an important role in antigen uptake and presentation and have been shown to mediate cellular interactions. The ligand specificity of the human macrophage galactose-type lectin (MGL) has been characterized extensively. Here, we set out to determine the glycan specificity of the murine homologues, MGL1 and MGL2, using a glycan array. Murine MGL1 was found to be highly specific for Lewis X and Lewis A structures, whereas mMGL2, more similar to the human MGL, recognized N-actetylgalactosamine (GalNAc) and galactose, including the O-linked Tn-antigen, TF-antigen and core 2. The generation of MGL1 and MGL2-Fc proteins allowed us to identify ligands in lymph nodes, and MGL1-Fc additionally recognized high endothelial venules. Strikingly, MGL2 interacted strongly to adenocarcinoma cells, suggesting a potential role in tumor immunity.</description><subject>Adenocarcinoma - metabolism</subject><subject>Animals</subject><subject>Antigen presenting cells</subject><subject>Antigen-Presenting Cells - immunology</subject><subject>Asialoglycoproteins - genetics</subject><subject>Asialoglycoproteins - immunology</subject><subject>Asialoglycoproteins - metabolism</subject><subject>Bone Marrow Cells - metabolism</subject><subject>C-type lectins</subject><subject>Carbohydrate recognition</subject><subject>Cell Line, Tumor</subject><subject>Cells, Cultured</subject><subject>Endothelium, Vascular - metabolism</subject><subject>Extracellular Matrix - metabolism</subject><subject>Lectins, C-Type - genetics</subject><subject>Lectins, C-Type - immunology</subject><subject>Lectins, C-Type - metabolism</subject><subject>Ligands</subject><subject>Lymph Nodes - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - immunology</subject><subject>Membrane Proteins - metabolism</subject><subject>MGL</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Polysaccharides - metabolism</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Skin - metabolism</subject><issn>0161-5890</issn><issn>1872-9142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE2LFDEQhoMo7rj6D0Ry8tZtKulPD4KMugojXvQc0unKWkN3uk3SC-OvN-MMePNUBfW8VdTD2EsQJQho3hzLeZlonkspRFcClELCI7aDrpVFD5V8zHYZg6LuenHDnsV4FEI0oqmfshvooZFKNjsW9z9NMDZhoN8m0eL54vi8BfLIv94dgBs_nhvJ90U6rcgntIl8fMs_UMyNTfx-OlnjeVzRkiNLiTD-jaVtXgIfyI_k7_kalhXDeficPXFmivjiWm_Zj08fv-8_F4dvd1_27w-FrWSTikp2I1jVD062qIzrnBygMsZBXVkUytVqqJ10Ak0Ptm6NgqEbpXFCDQ0qULfs9WVvPv1rw5j0TNHiNBmPyxZ10woh267LYHUBbVhiDOj0Gmg24aRB6LNsfdQX2fosWwPoLDvHXl33b8OM47_Q1W4G3l0AzF8-EAYdLaG3OFLIGvW40P8v_AH6VJPA</recordid><startdate>200903</startdate><enddate>200903</enddate><creator>Singh, Satwinder Kaur</creator><creator>Streng-Ouwehand, Ingeborg</creator><creator>Litjens, Manja</creator><creator>Weelij, Danny R.</creator><creator>García-Vallejo, Juan Jesús</creator><creator>van Vliet, Sandra J.</creator><creator>Saeland, Eirikur</creator><creator>van Kooyk, Yvette</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200903</creationdate><title>Characterization of murine MGL1 and MGL2 C-type lectins: Distinct glycan specificities and tumor binding properties</title><author>Singh, Satwinder Kaur ; Streng-Ouwehand, Ingeborg ; Litjens, Manja ; Weelij, Danny R. ; García-Vallejo, Juan Jesús ; van Vliet, Sandra J. ; Saeland, Eirikur ; van Kooyk, Yvette</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-428d1c39bf27e3af8f2b14aaf154ce03f53b5f2f0ea91c57a31b8d2af03b6e313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Adenocarcinoma - metabolism</topic><topic>Animals</topic><topic>Antigen presenting cells</topic><topic>Antigen-Presenting Cells - immunology</topic><topic>Asialoglycoproteins - genetics</topic><topic>Asialoglycoproteins - immunology</topic><topic>Asialoglycoproteins - metabolism</topic><topic>Bone Marrow Cells - metabolism</topic><topic>C-type lectins</topic><topic>Carbohydrate recognition</topic><topic>Cell Line, Tumor</topic><topic>Cells, Cultured</topic><topic>Endothelium, Vascular - metabolism</topic><topic>Extracellular Matrix - metabolism</topic><topic>Lectins, C-Type - genetics</topic><topic>Lectins, C-Type - immunology</topic><topic>Lectins, C-Type - metabolism</topic><topic>Ligands</topic><topic>Lymph Nodes - metabolism</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - immunology</topic><topic>Membrane Proteins - metabolism</topic><topic>MGL</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Polysaccharides - metabolism</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Skin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Singh, Satwinder Kaur</creatorcontrib><creatorcontrib>Streng-Ouwehand, Ingeborg</creatorcontrib><creatorcontrib>Litjens, Manja</creatorcontrib><creatorcontrib>Weelij, Danny R.</creatorcontrib><creatorcontrib>García-Vallejo, Juan Jesús</creatorcontrib><creatorcontrib>van Vliet, Sandra J.</creatorcontrib><creatorcontrib>Saeland, Eirikur</creatorcontrib><creatorcontrib>van Kooyk, Yvette</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Singh, Satwinder Kaur</au><au>Streng-Ouwehand, Ingeborg</au><au>Litjens, Manja</au><au>Weelij, Danny R.</au><au>García-Vallejo, Juan Jesús</au><au>van Vliet, Sandra J.</au><au>Saeland, Eirikur</au><au>van Kooyk, Yvette</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of murine MGL1 and MGL2 C-type lectins: Distinct glycan specificities and tumor binding properties</atitle><jtitle>Molecular immunology</jtitle><addtitle>Mol Immunol</addtitle><date>2009-03</date><risdate>2009</risdate><volume>46</volume><issue>6</issue><spage>1240</spage><epage>1249</epage><pages>1240-1249</pages><issn>0161-5890</issn><eissn>1872-9142</eissn><abstract>Antigen presenting cells (APC) express a variety of pattern recognition receptors, including the C-type lectin receptors (CLR) that specifically recognize carbohydrate structures expressed on self-tissue and pathogens. The CLR play an important role in antigen uptake and presentation and have been shown to mediate cellular interactions. The ligand specificity of the human macrophage galactose-type lectin (MGL) has been characterized extensively. Here, we set out to determine the glycan specificity of the murine homologues, MGL1 and MGL2, using a glycan array. Murine MGL1 was found to be highly specific for Lewis X and Lewis A structures, whereas mMGL2, more similar to the human MGL, recognized N-actetylgalactosamine (GalNAc) and galactose, including the O-linked Tn-antigen, TF-antigen and core 2. The generation of MGL1 and MGL2-Fc proteins allowed us to identify ligands in lymph nodes, and MGL1-Fc additionally recognized high endothelial venules. Strikingly, MGL2 interacted strongly to adenocarcinoma cells, suggesting a potential role in tumor immunity.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>19162326</pmid><doi>10.1016/j.molimm.2008.11.021</doi><tpages>10</tpages></addata></record> |
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| subjects | Adenocarcinoma - metabolism Animals Antigen presenting cells Antigen-Presenting Cells - immunology Asialoglycoproteins - genetics Asialoglycoproteins - immunology Asialoglycoproteins - metabolism Bone Marrow Cells - metabolism C-type lectins Carbohydrate recognition Cell Line, Tumor Cells, Cultured Endothelium, Vascular - metabolism Extracellular Matrix - metabolism Lectins, C-Type - genetics Lectins, C-Type - immunology Lectins, C-Type - metabolism Ligands Lymph Nodes - metabolism Membrane Proteins - genetics Membrane Proteins - immunology Membrane Proteins - metabolism MGL Mice Mice, Inbred C57BL Polysaccharides - metabolism Recombinant Proteins - genetics Recombinant Proteins - metabolism Skin - metabolism |
| title | Characterization of murine MGL1 and MGL2 C-type lectins: Distinct glycan specificities and tumor binding properties |
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