Characterizing CEACAM5 interaction with CD8α and CD1d in intestinal homeostasis
Normal intestinal epithelial cells (IECs) could act as non-professional antigen-presenting cells, selectively activating CD8 + -suppressor T cells. An epithelial cell surface glycoprotein, gp180, recognized by monoclonal antibodies B9 and L12 was determined to be critical in this process. Purificati...
Gespeichert in:
| Veröffentlicht in: | Mucosal immunology 2014-05, Vol.7 (3), p.615-624 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 624 |
|---|---|
| container_issue | 3 |
| container_start_page | 615 |
| container_title | Mucosal immunology |
| container_volume | 7 |
| creator | Roda, G Jianyu, X Park, M S DeMarte, L Hovhannisyan, Z Couri, R Stanners, C P Yeretssian, G Mayer, L |
| description | Normal intestinal epithelial cells (IECs) could act as non-professional antigen-presenting cells, selectively activating CD8
+
-suppressor T cells. An epithelial cell surface glycoprotein, gp180, recognized by monoclonal antibodies B9 and L12 was determined to be critical in this process. Purification and sequence analysis of mAb B9 reactive material revealed amino-acid sequence homology with CEACAM5. We demonstrate that CEACAM5 has properties attributed to gp180, such as CD8α binding and activation of CD8-associated Lck. CEACAM5 is the only CEACAM member interacting with CD1d through the B3 domain. Its N domain (recognized by B9) is required for CD8α binding. Removal of the N-domain glycosylated residues reduces B9 recognition, CD8α binding affinity, and activation of LcK. Therefore, conformational changes in CEACAM5 glycosylation site are critical for its interaction with CD8α. CEACAM5-activated CD8
+
T cells acquire the ability to suppress the proliferation of CD4
+
T cells
in vitro
in the presence of interleukin (IL)-15 or IL-7. We provide new insights into the role of CEACAM5 and define its specific immunoregulatory properties among the CEACAMs expressed on IECs. We suggest that unique set of interactions between CEACAM5, CD1d, and CD8 render CD1d more class I-like molecule, facilitating antigen presentation and activation of CD8
+
-suppressor regulatory T cells. |
| doi_str_mv | 10.1038/mi.2013.80 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3981948</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1519254296</sourcerecordid><originalsourceid>FETCH-LOGICAL-c344t-f9775906dc85cb91f64549564c8985b031b417969963d37a5fda3952d4c3eb293</originalsourceid><addsrcrecordid>eNptkc9OAyEQxonRWK1efACzR6PZCgts4WLSrH-TGj3ombAs29LsQoWtRt_KF_GZxLYaTTzNZL7ffAwzABwgOEAQs9PWDDKI8IDBDbCDOKYpJjTfXOY4hRniPbAbwgzCHEKKt0EvIwgSQtkOuC-m0kvVaW_ejJ0kxcWoGN3SxNhYinXjbPJiumlSnLOP90TaKmaoivoSCZ2xskmmrtUudDKYsAe2atkEvb-OffB4efFQXKfju6ubYjROFSakS2s-HFIO80oxqkqO6pxQwmlOFOOMlhCjkqAhzznPcYWHktaVxJxmFVFYlxnHfXC28p0vylZXStvOy0bMvWmlfxVOGvFXsWYqJu5ZYM4QJywaHK0NvHtaxJ-I1gSlm0Za7RZBIIp4RkkWB-iD4xWqvAvB6_rnGQTF1wliq_g6gWAwwoe_B_tBv3cegZMVEKJkJ9qLmVv4uMbwn90n_66PeQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1519254296</pqid></control><display><type>article</type><title>Characterizing CEACAM5 interaction with CD8α and CD1d in intestinal homeostasis</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Roda, G ; Jianyu, X ; Park, M S ; DeMarte, L ; Hovhannisyan, Z ; Couri, R ; Stanners, C P ; Yeretssian, G ; Mayer, L</creator><creatorcontrib>Roda, G ; Jianyu, X ; Park, M S ; DeMarte, L ; Hovhannisyan, Z ; Couri, R ; Stanners, C P ; Yeretssian, G ; Mayer, L</creatorcontrib><description>Normal intestinal epithelial cells (IECs) could act as non-professional antigen-presenting cells, selectively activating CD8
+
-suppressor T cells. An epithelial cell surface glycoprotein, gp180, recognized by monoclonal antibodies B9 and L12 was determined to be critical in this process. Purification and sequence analysis of mAb B9 reactive material revealed amino-acid sequence homology with CEACAM5. We demonstrate that CEACAM5 has properties attributed to gp180, such as CD8α binding and activation of CD8-associated Lck. CEACAM5 is the only CEACAM member interacting with CD1d through the B3 domain. Its N domain (recognized by B9) is required for CD8α binding. Removal of the N-domain glycosylated residues reduces B9 recognition, CD8α binding affinity, and activation of LcK. Therefore, conformational changes in CEACAM5 glycosylation site are critical for its interaction with CD8α. CEACAM5-activated CD8
+
T cells acquire the ability to suppress the proliferation of CD4
+
T cells
in vitro
in the presence of interleukin (IL)-15 or IL-7. We provide new insights into the role of CEACAM5 and define its specific immunoregulatory properties among the CEACAMs expressed on IECs. We suggest that unique set of interactions between CEACAM5, CD1d, and CD8 render CD1d more class I-like molecule, facilitating antigen presentation and activation of CD8
+
-suppressor regulatory T cells.</description><identifier>ISSN: 1933-0219</identifier><identifier>EISSN: 1935-3456</identifier><identifier>DOI: 10.1038/mi.2013.80</identifier><identifier>PMID: 24104458</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/250/1619/554/1834 ; 631/250/21/1293 ; 631/250/347 ; Allergology ; Amino Acid Sequence ; Animals ; Antibodies ; Antigens, CD1d - metabolism ; Biomedical and Life Sciences ; Biomedicine ; Carcinoembryonic Antigen - chemistry ; Carcinoembryonic Antigen - genetics ; Carcinoembryonic Antigen - metabolism ; CD8 Antigens - metabolism ; CD8-Positive T-Lymphocytes - immunology ; CD8-Positive T-Lymphocytes - metabolism ; Cell Line ; Epitopes - chemistry ; Epitopes - immunology ; Gastroenterology ; Glycosylation ; GPI-Linked Proteins - chemistry ; GPI-Linked Proteins - genetics ; GPI-Linked Proteins - metabolism ; Homeostasis ; Humans ; Immunology ; Intestinal Mucosa - metabolism ; Intestines - immunology ; Lymphocyte Activation - immunology ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism ; Models, Biological ; Molecular Sequence Data ; Multigene Family ; Phosphorylation ; Protein Interaction Domains and Motifs ; Sequence Alignment</subject><ispartof>Mucosal immunology, 2014-05, Vol.7 (3), p.615-624</ispartof><rights>Society for Mucosal Immunology 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c344t-f9775906dc85cb91f64549564c8985b031b417969963d37a5fda3952d4c3eb293</citedby><cites>FETCH-LOGICAL-c344t-f9775906dc85cb91f64549564c8985b031b417969963d37a5fda3952d4c3eb293</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27902,27903</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24104458$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Roda, G</creatorcontrib><creatorcontrib>Jianyu, X</creatorcontrib><creatorcontrib>Park, M S</creatorcontrib><creatorcontrib>DeMarte, L</creatorcontrib><creatorcontrib>Hovhannisyan, Z</creatorcontrib><creatorcontrib>Couri, R</creatorcontrib><creatorcontrib>Stanners, C P</creatorcontrib><creatorcontrib>Yeretssian, G</creatorcontrib><creatorcontrib>Mayer, L</creatorcontrib><title>Characterizing CEACAM5 interaction with CD8α and CD1d in intestinal homeostasis</title><title>Mucosal immunology</title><addtitle>Mucosal Immunol</addtitle><addtitle>Mucosal Immunol</addtitle><description>Normal intestinal epithelial cells (IECs) could act as non-professional antigen-presenting cells, selectively activating CD8
+
-suppressor T cells. An epithelial cell surface glycoprotein, gp180, recognized by monoclonal antibodies B9 and L12 was determined to be critical in this process. Purification and sequence analysis of mAb B9 reactive material revealed amino-acid sequence homology with CEACAM5. We demonstrate that CEACAM5 has properties attributed to gp180, such as CD8α binding and activation of CD8-associated Lck. CEACAM5 is the only CEACAM member interacting with CD1d through the B3 domain. Its N domain (recognized by B9) is required for CD8α binding. Removal of the N-domain glycosylated residues reduces B9 recognition, CD8α binding affinity, and activation of LcK. Therefore, conformational changes in CEACAM5 glycosylation site are critical for its interaction with CD8α. CEACAM5-activated CD8
+
T cells acquire the ability to suppress the proliferation of CD4
+
T cells
in vitro
in the presence of interleukin (IL)-15 or IL-7. We provide new insights into the role of CEACAM5 and define its specific immunoregulatory properties among the CEACAMs expressed on IECs. We suggest that unique set of interactions between CEACAM5, CD1d, and CD8 render CD1d more class I-like molecule, facilitating antigen presentation and activation of CD8
+
-suppressor regulatory T cells.</description><subject>631/250/1619/554/1834</subject><subject>631/250/21/1293</subject><subject>631/250/347</subject><subject>Allergology</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antigens, CD1d - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Carcinoembryonic Antigen - chemistry</subject><subject>Carcinoembryonic Antigen - genetics</subject><subject>Carcinoembryonic Antigen - metabolism</subject><subject>CD8 Antigens - metabolism</subject><subject>CD8-Positive T-Lymphocytes - immunology</subject><subject>CD8-Positive T-Lymphocytes - metabolism</subject><subject>Cell Line</subject><subject>Epitopes - chemistry</subject><subject>Epitopes - immunology</subject><subject>Gastroenterology</subject><subject>Glycosylation</subject><subject>GPI-Linked Proteins - chemistry</subject><subject>GPI-Linked Proteins - genetics</subject><subject>GPI-Linked Proteins - metabolism</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Immunology</subject><subject>Intestinal Mucosa - metabolism</subject><subject>Intestines - immunology</subject><subject>Lymphocyte Activation - immunology</subject><subject>Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>Phosphorylation</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Sequence Alignment</subject><issn>1933-0219</issn><issn>1935-3456</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkc9OAyEQxonRWK1efACzR6PZCgts4WLSrH-TGj3ombAs29LsQoWtRt_KF_GZxLYaTTzNZL7ffAwzABwgOEAQs9PWDDKI8IDBDbCDOKYpJjTfXOY4hRniPbAbwgzCHEKKt0EvIwgSQtkOuC-m0kvVaW_ejJ0kxcWoGN3SxNhYinXjbPJiumlSnLOP90TaKmaoivoSCZ2xskmmrtUudDKYsAe2atkEvb-OffB4efFQXKfju6ubYjROFSakS2s-HFIO80oxqkqO6pxQwmlOFOOMlhCjkqAhzznPcYWHktaVxJxmFVFYlxnHfXC28p0vylZXStvOy0bMvWmlfxVOGvFXsWYqJu5ZYM4QJywaHK0NvHtaxJ-I1gSlm0Za7RZBIIp4RkkWB-iD4xWqvAvB6_rnGQTF1wliq_g6gWAwwoe_B_tBv3cegZMVEKJkJ9qLmVv4uMbwn90n_66PeQ</recordid><startdate>20140501</startdate><enddate>20140501</enddate><creator>Roda, G</creator><creator>Jianyu, X</creator><creator>Park, M S</creator><creator>DeMarte, L</creator><creator>Hovhannisyan, Z</creator><creator>Couri, R</creator><creator>Stanners, C P</creator><creator>Yeretssian, G</creator><creator>Mayer, L</creator><general>Nature Publishing Group US</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><scope>5PM</scope></search><sort><creationdate>20140501</creationdate><title>Characterizing CEACAM5 interaction with CD8α and CD1d in intestinal homeostasis</title><author>Roda, G ; Jianyu, X ; Park, M S ; DeMarte, L ; Hovhannisyan, Z ; Couri, R ; Stanners, C P ; Yeretssian, G ; Mayer, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c344t-f9775906dc85cb91f64549564c8985b031b417969963d37a5fda3952d4c3eb293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>631/250/1619/554/1834</topic><topic>631/250/21/1293</topic><topic>631/250/347</topic><topic>Allergology</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antigens, CD1d - metabolism</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Carcinoembryonic Antigen - chemistry</topic><topic>Carcinoembryonic Antigen - genetics</topic><topic>Carcinoembryonic Antigen - metabolism</topic><topic>CD8 Antigens - metabolism</topic><topic>CD8-Positive T-Lymphocytes - immunology</topic><topic>CD8-Positive T-Lymphocytes - metabolism</topic><topic>Cell Line</topic><topic>Epitopes - chemistry</topic><topic>Epitopes - immunology</topic><topic>Gastroenterology</topic><topic>Glycosylation</topic><topic>GPI-Linked Proteins - chemistry</topic><topic>GPI-Linked Proteins - genetics</topic><topic>GPI-Linked Proteins - metabolism</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Immunology</topic><topic>Intestinal Mucosa - metabolism</topic><topic>Intestines - immunology</topic><topic>Lymphocyte Activation - immunology</topic><topic>Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism</topic><topic>Models, Biological</topic><topic>Molecular Sequence Data</topic><topic>Multigene Family</topic><topic>Phosphorylation</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roda, G</creatorcontrib><creatorcontrib>Jianyu, X</creatorcontrib><creatorcontrib>Park, M S</creatorcontrib><creatorcontrib>DeMarte, L</creatorcontrib><creatorcontrib>Hovhannisyan, Z</creatorcontrib><creatorcontrib>Couri, R</creatorcontrib><creatorcontrib>Stanners, C P</creatorcontrib><creatorcontrib>Yeretssian, G</creatorcontrib><creatorcontrib>Mayer, L</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Mucosal immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Roda, G</au><au>Jianyu, X</au><au>Park, M S</au><au>DeMarte, L</au><au>Hovhannisyan, Z</au><au>Couri, R</au><au>Stanners, C P</au><au>Yeretssian, G</au><au>Mayer, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterizing CEACAM5 interaction with CD8α and CD1d in intestinal homeostasis</atitle><jtitle>Mucosal immunology</jtitle><stitle>Mucosal Immunol</stitle><addtitle>Mucosal Immunol</addtitle><date>2014-05-01</date><risdate>2014</risdate><volume>7</volume><issue>3</issue><spage>615</spage><epage>624</epage><pages>615-624</pages><issn>1933-0219</issn><eissn>1935-3456</eissn><abstract>Normal intestinal epithelial cells (IECs) could act as non-professional antigen-presenting cells, selectively activating CD8
+
-suppressor T cells. An epithelial cell surface glycoprotein, gp180, recognized by monoclonal antibodies B9 and L12 was determined to be critical in this process. Purification and sequence analysis of mAb B9 reactive material revealed amino-acid sequence homology with CEACAM5. We demonstrate that CEACAM5 has properties attributed to gp180, such as CD8α binding and activation of CD8-associated Lck. CEACAM5 is the only CEACAM member interacting with CD1d through the B3 domain. Its N domain (recognized by B9) is required for CD8α binding. Removal of the N-domain glycosylated residues reduces B9 recognition, CD8α binding affinity, and activation of LcK. Therefore, conformational changes in CEACAM5 glycosylation site are critical for its interaction with CD8α. CEACAM5-activated CD8
+
T cells acquire the ability to suppress the proliferation of CD4
+
T cells
in vitro
in the presence of interleukin (IL)-15 or IL-7. We provide new insights into the role of CEACAM5 and define its specific immunoregulatory properties among the CEACAMs expressed on IECs. We suggest that unique set of interactions between CEACAM5, CD1d, and CD8 render CD1d more class I-like molecule, facilitating antigen presentation and activation of CD8
+
-suppressor regulatory T cells.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>24104458</pmid><doi>10.1038/mi.2013.80</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1933-0219 |
| ispartof | Mucosal immunology, 2014-05, Vol.7 (3), p.615-624 |
| issn | 1933-0219 1935-3456 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3981948 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | 631/250/1619/554/1834 631/250/21/1293 631/250/347 Allergology Amino Acid Sequence Animals Antibodies Antigens, CD1d - metabolism Biomedical and Life Sciences Biomedicine Carcinoembryonic Antigen - chemistry Carcinoembryonic Antigen - genetics Carcinoembryonic Antigen - metabolism CD8 Antigens - metabolism CD8-Positive T-Lymphocytes - immunology CD8-Positive T-Lymphocytes - metabolism Cell Line Epitopes - chemistry Epitopes - immunology Gastroenterology Glycosylation GPI-Linked Proteins - chemistry GPI-Linked Proteins - genetics GPI-Linked Proteins - metabolism Homeostasis Humans Immunology Intestinal Mucosa - metabolism Intestines - immunology Lymphocyte Activation - immunology Lymphocyte Specific Protein Tyrosine Kinase p56(lck) - metabolism Models, Biological Molecular Sequence Data Multigene Family Phosphorylation Protein Interaction Domains and Motifs Sequence Alignment |
| title | Characterizing CEACAM5 interaction with CD8α and CD1d in intestinal homeostasis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T08%3A53%3A13IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterizing%20CEACAM5%20interaction%20with%20CD8%CE%B1%20and%20CD1d%20in%20intestinal%20homeostasis&rft.jtitle=Mucosal%20immunology&rft.au=Roda,%20G&rft.date=2014-05-01&rft.volume=7&rft.issue=3&rft.spage=615&rft.epage=624&rft.pages=615-624&rft.issn=1933-0219&rft.eissn=1935-3456&rft_id=info:doi/10.1038/mi.2013.80&rft_dat=%3Cproquest_pubme%3E1519254296%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1519254296&rft_id=info:pmid/24104458&rfr_iscdi=true |