Analysis of the binding of gluten T-cell epitopes to various human leukocyte antigen class II molecules
Summary Celiac disease is a prevalent disorder of the small intestine that is caused by an inflammatory reaction to dietary gluten in genetically susceptible individuals. More than 90% of patients express the HLA-DQ2 molecule, whereas DQ8 is carried by most of the remaining patients. DQ2- and DQ8-me...
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| Veröffentlicht in: | Human immunology 2008-02, Vol.69 (2), p.94-100 |
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| creator | Bergseng, Elin Sidney, John Sette, Alessandro Sollid, Ludvig M |
| description | Summary Celiac disease is a prevalent disorder of the small intestine that is caused by an inflammatory reaction to dietary gluten in genetically susceptible individuals. More than 90% of patients express the HLA-DQ2 molecule, whereas DQ8 is carried by most of the remaining patients. DQ2- and DQ8-mediated presentation of gluten peptides to CD4+ T cells is a key event in the pathogenesis of the disease. The association of celiac disease with these human leukocyte antigen (HLA) molecules is explained by a preferential binding of gluten peptides to these HLA molecules, although the actual data on this in the literature are scarce. The objective of this study was to test this hypothesis. A panel of peptides representing DQ2-restricted gluten T-cell epitopes was tested for binding to various HLA class II molecules using various experimental approaches. The results demonstrate that the gluten T-cell epitopes mainly bind to the DQ2 molecule. |
| doi_str_mv | 10.1016/j.humimm.2008.01.002 |
| format | Article |
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More than 90% of patients express the HLA-DQ2 molecule, whereas DQ8 is carried by most of the remaining patients. DQ2- and DQ8-mediated presentation of gluten peptides to CD4+ T cells is a key event in the pathogenesis of the disease. The association of celiac disease with these human leukocyte antigen (HLA) molecules is explained by a preferential binding of gluten peptides to these HLA molecules, although the actual data on this in the literature are scarce. The objective of this study was to test this hypothesis. A panel of peptides representing DQ2-restricted gluten T-cell epitopes was tested for binding to various HLA class II molecules using various experimental approaches. The results demonstrate that the gluten T-cell epitopes mainly bind to the DQ2 molecule.</description><identifier>ISSN: 0198-8859</identifier><identifier>EISSN: 1879-1166</identifier><identifier>DOI: 10.1016/j.humimm.2008.01.002</identifier><identifier>PMID: 18361933</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Allergy and Immunology ; Antigen Presentation - immunology ; Binding Sites ; Binding, Competitive ; CD4-Positive T-Lymphocytes - immunology ; CD4-Positive T-Lymphocytes - metabolism ; Celiac disease ; Celiac Disease - immunology ; DQ2 ; Epitopes, T-Lymphocyte - immunology ; Epitopes, T-Lymphocyte - metabolism ; Genetic Predisposition to Disease ; Gluten T-cell epitopes ; Glutens - chemistry ; Glutens - immunology ; Glutens - metabolism ; HLA class II molecules ; HLA-D Antigens - immunology ; HLA-D Antigens - metabolism ; HLA-DQ Antigens - immunology ; HLA-DQ Antigens - metabolism ; Humans ; Hydrogen Bonding ; Peptide binding ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; Peptide Fragments - metabolism ; Radioligand Assay</subject><ispartof>Human immunology, 2008-02, Vol.69 (2), p.94-100</ispartof><rights>American Society for Histocompatibility and Immunogenetics</rights><rights>2008 American Society for Histocompatibility and Immunogenetics</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-30186c4d40d466dcd06365c60eefbc861f200630d8661887a23fb15f7f6b19b93</citedby><cites>FETCH-LOGICAL-c446t-30186c4d40d466dcd06365c60eefbc861f200630d8661887a23fb15f7f6b19b93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.humimm.2008.01.002$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3549,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18361933$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bergseng, Elin</creatorcontrib><creatorcontrib>Sidney, John</creatorcontrib><creatorcontrib>Sette, Alessandro</creatorcontrib><creatorcontrib>Sollid, Ludvig M</creatorcontrib><title>Analysis of the binding of gluten T-cell epitopes to various human leukocyte antigen class II molecules</title><title>Human immunology</title><addtitle>Hum Immunol</addtitle><description>Summary Celiac disease is a prevalent disorder of the small intestine that is caused by an inflammatory reaction to dietary gluten in genetically susceptible individuals. More than 90% of patients express the HLA-DQ2 molecule, whereas DQ8 is carried by most of the remaining patients. DQ2- and DQ8-mediated presentation of gluten peptides to CD4+ T cells is a key event in the pathogenesis of the disease. The association of celiac disease with these human leukocyte antigen (HLA) molecules is explained by a preferential binding of gluten peptides to these HLA molecules, although the actual data on this in the literature are scarce. The objective of this study was to test this hypothesis. A panel of peptides representing DQ2-restricted gluten T-cell epitopes was tested for binding to various HLA class II molecules using various experimental approaches. The results demonstrate that the gluten T-cell epitopes mainly bind to the DQ2 molecule.</description><subject>Allergy and Immunology</subject><subject>Antigen Presentation - immunology</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>CD4-Positive T-Lymphocytes - immunology</subject><subject>CD4-Positive T-Lymphocytes - metabolism</subject><subject>Celiac disease</subject><subject>Celiac Disease - immunology</subject><subject>DQ2</subject><subject>Epitopes, T-Lymphocyte - immunology</subject><subject>Epitopes, T-Lymphocyte - metabolism</subject><subject>Genetic Predisposition to Disease</subject><subject>Gluten T-cell epitopes</subject><subject>Glutens - chemistry</subject><subject>Glutens - immunology</subject><subject>Glutens - metabolism</subject><subject>HLA class II molecules</subject><subject>HLA-D Antigens - immunology</subject><subject>HLA-D Antigens - metabolism</subject><subject>HLA-DQ Antigens - immunology</subject><subject>HLA-DQ Antigens - metabolism</subject><subject>Humans</subject><subject>Hydrogen Bonding</subject><subject>Peptide binding</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>Peptide Fragments - metabolism</subject><subject>Radioligand Assay</subject><issn>0198-8859</issn><issn>1879-1166</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUsFq3DAUFKWl2ab9g1J06s3uk619li-FENJ2IdBD07OQ5eeNNrK1lezA_n1ldqHQS04Pwcy80Zth7KOAUoDAL4fycRndOJYVgCpBlADVK7YRqmkLIRBfsw2IVhVKbdsr9i6lAwA00Mi37EqoGkVb1xu2v5mMPyWXeBj4_Ei8c1Pvpv363Ptlpok_FJa853R0czhS4nPgzya6sCSeHZiJe1qegj3NxM00u32mWG9S4rsdH4Mnu3hK79mbwfhEHy7zmv3-dvdw-6O4__l9d3tzX1gpcS5qEAqt7CX0ErG3PWCNW4tANHRWoRjyb7GGXiEKpRpT1UMntkMzYCfarq2v2eez7jGGPwulWY8urf7NRNmxbkBWzVbhi8AKELCtZAbKM9DGkFKkQR-jG008aQF6TUIf9DkJvSahQeicRKZ9uugv3Uj9P9Ll9Bnw9QygfI5nR1En62iy1LtIdtZ9cC9t-F_Aejc5a_wTnSgdwhJztkkLnSoN-tfahrUMoGBtgqz_ArzMsMM</recordid><startdate>20080201</startdate><enddate>20080201</enddate><creator>Bergseng, Elin</creator><creator>Sidney, John</creator><creator>Sette, Alessandro</creator><creator>Sollid, Ludvig M</creator><general>Elsevier Inc</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20080201</creationdate><title>Analysis of the binding of gluten T-cell epitopes to various human leukocyte antigen class II molecules</title><author>Bergseng, Elin ; Sidney, John ; Sette, Alessandro ; Sollid, Ludvig M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-30186c4d40d466dcd06365c60eefbc861f200630d8661887a23fb15f7f6b19b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Allergy and Immunology</topic><topic>Antigen Presentation - immunology</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>CD4-Positive T-Lymphocytes - immunology</topic><topic>CD4-Positive T-Lymphocytes - metabolism</topic><topic>Celiac disease</topic><topic>Celiac Disease - immunology</topic><topic>DQ2</topic><topic>Epitopes, T-Lymphocyte - immunology</topic><topic>Epitopes, T-Lymphocyte - metabolism</topic><topic>Genetic Predisposition to Disease</topic><topic>Gluten T-cell epitopes</topic><topic>Glutens - chemistry</topic><topic>Glutens - immunology</topic><topic>Glutens - metabolism</topic><topic>HLA class II molecules</topic><topic>HLA-D Antigens - immunology</topic><topic>HLA-D Antigens - metabolism</topic><topic>HLA-DQ Antigens - immunology</topic><topic>HLA-DQ Antigens - metabolism</topic><topic>Humans</topic><topic>Hydrogen Bonding</topic><topic>Peptide binding</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - immunology</topic><topic>Peptide Fragments - metabolism</topic><topic>Radioligand Assay</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bergseng, Elin</creatorcontrib><creatorcontrib>Sidney, John</creatorcontrib><creatorcontrib>Sette, Alessandro</creatorcontrib><creatorcontrib>Sollid, Ludvig M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Human immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bergseng, Elin</au><au>Sidney, John</au><au>Sette, Alessandro</au><au>Sollid, Ludvig M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the binding of gluten T-cell epitopes to various human leukocyte antigen class II molecules</atitle><jtitle>Human immunology</jtitle><addtitle>Hum Immunol</addtitle><date>2008-02-01</date><risdate>2008</risdate><volume>69</volume><issue>2</issue><spage>94</spage><epage>100</epage><pages>94-100</pages><issn>0198-8859</issn><eissn>1879-1166</eissn><abstract>Summary Celiac disease is a prevalent disorder of the small intestine that is caused by an inflammatory reaction to dietary gluten in genetically susceptible individuals. More than 90% of patients express the HLA-DQ2 molecule, whereas DQ8 is carried by most of the remaining patients. DQ2- and DQ8-mediated presentation of gluten peptides to CD4+ T cells is a key event in the pathogenesis of the disease. The association of celiac disease with these human leukocyte antigen (HLA) molecules is explained by a preferential binding of gluten peptides to these HLA molecules, although the actual data on this in the literature are scarce. The objective of this study was to test this hypothesis. A panel of peptides representing DQ2-restricted gluten T-cell epitopes was tested for binding to various HLA class II molecules using various experimental approaches. The results demonstrate that the gluten T-cell epitopes mainly bind to the DQ2 molecule.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18361933</pmid><doi>10.1016/j.humimm.2008.01.002</doi><tpages>7</tpages></addata></record> |
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| subjects | Allergy and Immunology Antigen Presentation - immunology Binding Sites Binding, Competitive CD4-Positive T-Lymphocytes - immunology CD4-Positive T-Lymphocytes - metabolism Celiac disease Celiac Disease - immunology DQ2 Epitopes, T-Lymphocyte - immunology Epitopes, T-Lymphocyte - metabolism Genetic Predisposition to Disease Gluten T-cell epitopes Glutens - chemistry Glutens - immunology Glutens - metabolism HLA class II molecules HLA-D Antigens - immunology HLA-D Antigens - metabolism HLA-DQ Antigens - immunology HLA-DQ Antigens - metabolism Humans Hydrogen Bonding Peptide binding Peptide Fragments - chemistry Peptide Fragments - immunology Peptide Fragments - metabolism Radioligand Assay |
| title | Analysis of the binding of gluten T-cell epitopes to various human leukocyte antigen class II molecules |
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