Sialylated multivalent antigens engage CD22 in trans and inhibit B cell activation
CD22 is an inhibitory coreceptor on the surface of B cells that attenuates B cell antigen receptor (BCR) signaling and, therefore, B cell activation. Elucidating the molecular mechanisms underlying the inhibitory activity of CD22 is complicated by the ubiquity of CD22 ligands. Although antigens can...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2009-02, Vol.106 (8), p.2500-2505 |
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| creator | Courtney, Adam H Puffer, Erik B Pontrello, Jason K Yang, Zhi-Qiang Kiessling, Laura L |
| description | CD22 is an inhibitory coreceptor on the surface of B cells that attenuates B cell antigen receptor (BCR) signaling and, therefore, B cell activation. Elucidating the molecular mechanisms underlying the inhibitory activity of CD22 is complicated by the ubiquity of CD22 ligands. Although antigens can display CD22 ligands, the receptor is known to bind to sialylated glycoproteins on the cell surface. The propinquity of CD22 and cell-surface glycoprotein ligands has led to the conclusion that the inhibitory properties of the receptor are due to cis interactions. Here, we examine the functional consequences of trans interactions by employing sialylated multivalent antigens that can engage both CD22 and the BCR. Exposure of B cells to sialylated antigens results in the inhibition of key steps in BCR signaling. These results reveal that antigens bearing CD22 ligands are powerful suppressors of B cell activation. The ability of sialylated antigens to inhibit BCR signaling through trans CD22 interactions reveals a previously unrecognized role for the Siglec-family of receptors as modulators of immune signaling. |
| doi_str_mv | 10.1073/pnas.0807207106 |
| format | Article |
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Elucidating the molecular mechanisms underlying the inhibitory activity of CD22 is complicated by the ubiquity of CD22 ligands. Although antigens can display CD22 ligands, the receptor is known to bind to sialylated glycoproteins on the cell surface. The propinquity of CD22 and cell-surface glycoprotein ligands has led to the conclusion that the inhibitory properties of the receptor are due to cis interactions. Here, we examine the functional consequences of trans interactions by employing sialylated multivalent antigens that can engage both CD22 and the BCR. Exposure of B cells to sialylated antigens results in the inhibition of key steps in BCR signaling. These results reveal that antigens bearing CD22 ligands are powerful suppressors of B cell activation. The ability of sialylated antigens to inhibit BCR signaling through trans CD22 interactions reveals a previously unrecognized role for the Siglec-family of receptors as modulators of immune signaling.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0807207106</identifier><identifier>PMID: 19202057</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Animals ; Antigens ; B lymphocytes ; B-Lymphocytes - immunology ; Biochemistry ; Biological Sciences ; Carbohydrate Sequence ; Cell Line ; Cells ; Copolymers ; Glycoconjugates ; Glycoproteins ; Humans ; Immune system ; Ligands ; Lymphocyte Activation - immunology ; Lymphocytes ; Molecular Sequence Data ; N-Acetylneuraminic Acid - chemistry ; Phosphorylation ; Physical Sciences ; Physiological regulation ; Polymers ; Receptors ; Sialic Acid Binding Ig-like Lectin 2 - chemistry ; Sialic Acid Binding Ig-like Lectin 2 - immunology ; Signal Transduction</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2009-02, Vol.106 (8), p.2500-2505</ispartof><rights>Copyright National Academy of Sciences Feb 24, 2009</rights><rights>2009 by The National Academy of Sciences of the USA</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c509t-abac38c8d2c87d8bf43f6737227ba6fec08e40010133ef4d673318c03dc8dd993</citedby><cites>FETCH-LOGICAL-c509t-abac38c8d2c87d8bf43f6737227ba6fec08e40010133ef4d673318c03dc8dd993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/106/8.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/40421737$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/40421737$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19202057$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Courtney, Adam H</creatorcontrib><creatorcontrib>Puffer, Erik B</creatorcontrib><creatorcontrib>Pontrello, Jason K</creatorcontrib><creatorcontrib>Yang, Zhi-Qiang</creatorcontrib><creatorcontrib>Kiessling, Laura L</creatorcontrib><title>Sialylated multivalent antigens engage CD22 in trans and inhibit B cell activation</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>CD22 is an inhibitory coreceptor on the surface of B cells that attenuates B cell antigen receptor (BCR) signaling and, therefore, B cell activation. Elucidating the molecular mechanisms underlying the inhibitory activity of CD22 is complicated by the ubiquity of CD22 ligands. Although antigens can display CD22 ligands, the receptor is known to bind to sialylated glycoproteins on the cell surface. The propinquity of CD22 and cell-surface glycoprotein ligands has led to the conclusion that the inhibitory properties of the receptor are due to cis interactions. Here, we examine the functional consequences of trans interactions by employing sialylated multivalent antigens that can engage both CD22 and the BCR. Exposure of B cells to sialylated antigens results in the inhibition of key steps in BCR signaling. These results reveal that antigens bearing CD22 ligands are powerful suppressors of B cell activation. The ability of sialylated antigens to inhibit BCR signaling through trans CD22 interactions reveals a previously unrecognized role for the Siglec-family of receptors as modulators of immune signaling.</description><subject>Animals</subject><subject>Antigens</subject><subject>B lymphocytes</subject><subject>B-Lymphocytes - immunology</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Carbohydrate Sequence</subject><subject>Cell Line</subject><subject>Cells</subject><subject>Copolymers</subject><subject>Glycoconjugates</subject><subject>Glycoproteins</subject><subject>Humans</subject><subject>Immune system</subject><subject>Ligands</subject><subject>Lymphocyte Activation - immunology</subject><subject>Lymphocytes</subject><subject>Molecular Sequence Data</subject><subject>N-Acetylneuraminic Acid - chemistry</subject><subject>Phosphorylation</subject><subject>Physical Sciences</subject><subject>Physiological regulation</subject><subject>Polymers</subject><subject>Receptors</subject><subject>Sialic Acid Binding Ig-like Lectin 2 - chemistry</subject><subject>Sialic Acid Binding Ig-like Lectin 2 - immunology</subject><subject>Signal Transduction</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhS0EotPCmhUQdQGrtNeP-LFBguEpVUKidG05jjP1KONMbaei_x5HM-oUhMTKss93ju71QegFhjMMgp5vg0lnIEEQEBj4I7TAoHDNmYLHaAFARC0ZYUfoOKU1AKhGwlN0hBUBAo1YoB-X3gx3g8muqzbTkP2tGVzIlQnZr1xIlQsrs3LV8iMhlQ9VjqY8mtCVy7Vvfa4-VNYNQ2Xs7M1-DM_Qk94MyT3fnyfo6vOnn8uv9cX3L9-W7y9q24DKtWmNpdLKjlgpOtn2jPZcUEGIaA3vnQXpGAAGTKnrWVc0iqUF2hVPpxQ9Qe92udup3bjOlrGjGfQ2-o2Jd3o0Xv-pBH-tV-OtJrwBokgJeLMPiOPN5FLWG5_mZUxw45Q056phTLD_guUzKW8wFPD0L3A9TjGUXygMLkUAxwU630E2jilF19-PjEHPreq5VX1otThePdz0wO9rLMDbPTA7D3FcS00aAN1Pw5Ddr_wg6t9kAV7ugHXKY7wnGDCCSztFf73TezNqs4o-6avLshwF3CjJyzC_AfySyAg</recordid><startdate>20090224</startdate><enddate>20090224</enddate><creator>Courtney, Adam H</creator><creator>Puffer, Erik B</creator><creator>Pontrello, Jason K</creator><creator>Yang, Zhi-Qiang</creator><creator>Kiessling, Laura L</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</scope><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090224</creationdate><title>Sialylated multivalent antigens engage CD22 in trans and inhibit B cell activation</title><author>Courtney, Adam H ; Puffer, Erik B ; Pontrello, Jason K ; Yang, Zhi-Qiang ; Kiessling, Laura L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c509t-abac38c8d2c87d8bf43f6737227ba6fec08e40010133ef4d673318c03dc8dd993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Antigens</topic><topic>B lymphocytes</topic><topic>B-Lymphocytes - immunology</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Carbohydrate Sequence</topic><topic>Cell Line</topic><topic>Cells</topic><topic>Copolymers</topic><topic>Glycoconjugates</topic><topic>Glycoproteins</topic><topic>Humans</topic><topic>Immune system</topic><topic>Ligands</topic><topic>Lymphocyte Activation - immunology</topic><topic>Lymphocytes</topic><topic>Molecular Sequence Data</topic><topic>N-Acetylneuraminic Acid - chemistry</topic><topic>Phosphorylation</topic><topic>Physical Sciences</topic><topic>Physiological regulation</topic><topic>Polymers</topic><topic>Receptors</topic><topic>Sialic Acid Binding Ig-like Lectin 2 - chemistry</topic><topic>Sialic Acid Binding Ig-like Lectin 2 - immunology</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Courtney, Adam H</creatorcontrib><creatorcontrib>Puffer, Erik B</creatorcontrib><creatorcontrib>Pontrello, Jason K</creatorcontrib><creatorcontrib>Yang, Zhi-Qiang</creatorcontrib><creatorcontrib>Kiessling, Laura L</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Courtney, Adam H</au><au>Puffer, Erik B</au><au>Pontrello, Jason K</au><au>Yang, Zhi-Qiang</au><au>Kiessling, Laura L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sialylated multivalent antigens engage CD22 in trans and inhibit B cell activation</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2009-02-24</date><risdate>2009</risdate><volume>106</volume><issue>8</issue><spage>2500</spage><epage>2505</epage><pages>2500-2505</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>CD22 is an inhibitory coreceptor on the surface of B cells that attenuates B cell antigen receptor (BCR) signaling and, therefore, B cell activation. 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| subjects | Animals Antigens B lymphocytes B-Lymphocytes - immunology Biochemistry Biological Sciences Carbohydrate Sequence Cell Line Cells Copolymers Glycoconjugates Glycoproteins Humans Immune system Ligands Lymphocyte Activation - immunology Lymphocytes Molecular Sequence Data N-Acetylneuraminic Acid - chemistry Phosphorylation Physical Sciences Physiological regulation Polymers Receptors Sialic Acid Binding Ig-like Lectin 2 - chemistry Sialic Acid Binding Ig-like Lectin 2 - immunology Signal Transduction |
| title | Sialylated multivalent antigens engage CD22 in trans and inhibit B cell activation |
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