Truncation analysis of several DR binding epitopes
Peptide regions crucial for binding to four different DR alleles (DR1, DR2, DR5, and DR52a) have been localized in five unrelated DR binding peptides (dynorphin 1-13, sperm whale myoglobin 132-153, influenza hemagglutinin 307-319, pigeon cytochrome c 88-104, and tetanus toxoid 830-843) by testing pa...
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| Veröffentlicht in: | The Journal of immunology (1950) 1991-02, Vol.146 (4), p.1240-1246 |
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| container_title | The Journal of immunology (1950) |
| container_volume | 146 |
| creator | O'Sullivan, D Sidney, J Del Guercio, MF Colon, SM Sette, A |
| description | Peptide regions crucial for binding to four different DR alleles (DR1, DR2, DR5, and DR52a) have been localized in five unrelated DR binding peptides (dynorphin 1-13, sperm whale myoglobin 132-153, influenza hemagglutinin 307-319, pigeon cytochrome c 88-104, and tetanus toxoid 830-843) by testing panels of truncated analogs for DR binding. It was found that in most cases, different DR alleles recognize almost identical, albeit distinct, core regions, suggesting that different DR alleles may recognize similar structures on their peptide ligands. Furthermore, it was found that these core regions, notwithstanding their derivation from unrelated sequences, share a common structural pattern. When the sequences of several other unrelated determinants were scrutinized, the structural motif identified was present in some, but absent in other good DR binders, suggesting that good DR binding capacity of peptide molecules may be compatible with more than one single sequence pattern. |
| doi_str_mv | 10.4049/jimmunol.146.4.1240 |
| format | Article |
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It was found that in most cases, different DR alleles recognize almost identical, albeit distinct, core regions, suggesting that different DR alleles may recognize similar structures on their peptide ligands. Furthermore, it was found that these core regions, notwithstanding their derivation from unrelated sequences, share a common structural pattern. When the sequences of several other unrelated determinants were scrutinized, the structural motif identified was present in some, but absent in other good DR binders, suggesting that good DR binding capacity of peptide molecules may be compatible with more than one single sequence pattern.</description><identifier>ISSN: 0022-1767</identifier><identifier>EISSN: 1550-6606</identifier><identifier>DOI: 10.4049/jimmunol.146.4.1240</identifier><identifier>PMID: 1704034</identifier><identifier>CODEN: JOIMA3</identifier><language>eng</language><publisher>Bethesda, MD: Am Assoc Immnol</publisher><subject>Alleles ; Amino Acid Sequence ; Antigenic determinants, haptens, artificial antigens ; Antigens ; Biological and medical sciences ; Cell Line, Transformed ; Dynorphins - immunology ; Epitopes - chemistry ; Epitopes - immunology ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral - immunology ; HLA-DR Antigens - immunology ; Humans ; Molecular immunology ; Molecular Sequence Data ; Myoglobin - immunology ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; Tetanus Toxoid - immunology</subject><ispartof>The Journal of immunology (1950), 1991-02, Vol.146 (4), p.1240-1246</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-72717ad33e9425e5401f44a7f1237c1af89a840e219abc9fcb170062b68b58593</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19715225$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1704034$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>O'Sullivan, D</creatorcontrib><creatorcontrib>Sidney, J</creatorcontrib><creatorcontrib>Del Guercio, MF</creatorcontrib><creatorcontrib>Colon, SM</creatorcontrib><creatorcontrib>Sette, A</creatorcontrib><title>Truncation analysis of several DR binding epitopes</title><title>The Journal of immunology (1950)</title><addtitle>J Immunol</addtitle><description>Peptide regions crucial for binding to four different DR alleles (DR1, DR2, DR5, and DR52a) have been localized in five unrelated DR binding peptides (dynorphin 1-13, sperm whale myoglobin 132-153, influenza hemagglutinin 307-319, pigeon cytochrome c 88-104, and tetanus toxoid 830-843) by testing panels of truncated analogs for DR binding. It was found that in most cases, different DR alleles recognize almost identical, albeit distinct, core regions, suggesting that different DR alleles may recognize similar structures on their peptide ligands. Furthermore, it was found that these core regions, notwithstanding their derivation from unrelated sequences, share a common structural pattern. When the sequences of several other unrelated determinants were scrutinized, the structural motif identified was present in some, but absent in other good DR binders, suggesting that good DR binding capacity of peptide molecules may be compatible with more than one single sequence pattern.</description><subject>Alleles</subject><subject>Amino Acid Sequence</subject><subject>Antigenic determinants, haptens, artificial antigens</subject><subject>Antigens</subject><subject>Biological and medical sciences</subject><subject>Cell Line, Transformed</subject><subject>Dynorphins - immunology</subject><subject>Epitopes - chemistry</subject><subject>Epitopes - immunology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus</subject><subject>Hemagglutinins, Viral - immunology</subject><subject>HLA-DR Antigens - immunology</subject><subject>Humans</subject><subject>Molecular immunology</subject><subject>Molecular Sequence Data</subject><subject>Myoglobin - immunology</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>Tetanus Toxoid - immunology</subject><issn>0022-1767</issn><issn>1550-6606</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EKqXwBQgpG2CVMnbGcbJE5SlVQkJlbTmu07pykmI3RP17UrUIdqxmMefeGR1CLimMETC_W9mqauvGjSmmYxxThnBEhpRziNMU0mMyBGAspiIVp-QshBUApMBwQAZUAEKCQ8Jmvq212timjlSt3DbYEDVlFMyX8cpFD-9RYeu5rReRWdtNszbhnJyUygVzcZgj8vH0OJu8xNO359fJ_TTWmGSbWDBBhZonicmRccMRaImoRElZIjRVZZarDMEwmqtC56Uu-qcgZUWaFTzjeTIiN_vetW8-WxM2srJBG-dUbZo2yAwwyZnAf0HKM8YF2zUme1D7JgRvSrn2tlJ-KynInVL5o1T2SiXKndI-dXWob4vKzH8ze4f9_vqwV0ErV3pVaxt-sVxQzhjvuds9t7SLZWe9kaFSzvWtVHZd9-fiN9KzjLc</recordid><startdate>19910215</startdate><enddate>19910215</enddate><creator>O'Sullivan, D</creator><creator>Sidney, J</creator><creator>Del Guercio, MF</creator><creator>Colon, SM</creator><creator>Sette, A</creator><general>Am Assoc Immnol</general><general>American Association of Immunologists</general><scope>IQODW</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19910215</creationdate><title>Truncation analysis of several DR binding epitopes</title><author>O'Sullivan, D ; Sidney, J ; Del Guercio, MF ; Colon, SM ; Sette, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-72717ad33e9425e5401f44a7f1237c1af89a840e219abc9fcb170062b68b58593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Alleles</topic><topic>Amino Acid Sequence</topic><topic>Antigenic determinants, haptens, artificial antigens</topic><topic>Antigens</topic><topic>Biological and medical sciences</topic><topic>Cell Line, Transformed</topic><topic>Dynorphins - immunology</topic><topic>Epitopes - chemistry</topic><topic>Epitopes - immunology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus</topic><topic>Hemagglutinins, Viral - immunology</topic><topic>HLA-DR Antigens - immunology</topic><topic>Humans</topic><topic>Molecular immunology</topic><topic>Molecular Sequence Data</topic><topic>Myoglobin - immunology</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - immunology</topic><topic>Tetanus Toxoid - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>O'Sullivan, D</creatorcontrib><creatorcontrib>Sidney, J</creatorcontrib><creatorcontrib>Del Guercio, MF</creatorcontrib><creatorcontrib>Colon, SM</creatorcontrib><creatorcontrib>Sette, A</creatorcontrib><collection>Pascal-Francis</collection><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>The Journal of immunology (1950)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>O'Sullivan, D</au><au>Sidney, J</au><au>Del Guercio, MF</au><au>Colon, SM</au><au>Sette, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Truncation analysis of several DR binding epitopes</atitle><jtitle>The Journal of immunology (1950)</jtitle><addtitle>J Immunol</addtitle><date>1991-02-15</date><risdate>1991</risdate><volume>146</volume><issue>4</issue><spage>1240</spage><epage>1246</epage><pages>1240-1246</pages><issn>0022-1767</issn><eissn>1550-6606</eissn><coden>JOIMA3</coden><abstract>Peptide regions crucial for binding to four different DR alleles (DR1, DR2, DR5, and DR52a) have been localized in five unrelated DR binding peptides (dynorphin 1-13, sperm whale myoglobin 132-153, influenza hemagglutinin 307-319, pigeon cytochrome c 88-104, and tetanus toxoid 830-843) by testing panels of truncated analogs for DR binding. It was found that in most cases, different DR alleles recognize almost identical, albeit distinct, core regions, suggesting that different DR alleles may recognize similar structures on their peptide ligands. Furthermore, it was found that these core regions, notwithstanding their derivation from unrelated sequences, share a common structural pattern. When the sequences of several other unrelated determinants were scrutinized, the structural motif identified was present in some, but absent in other good DR binders, suggesting that good DR binding capacity of peptide molecules may be compatible with more than one single sequence pattern.</abstract><cop>Bethesda, MD</cop><pub>Am Assoc Immnol</pub><pmid>1704034</pmid><doi>10.4049/jimmunol.146.4.1240</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of immunology (1950), 1991-02, Vol.146 (4), p.1240-1246 |
| issn | 0022-1767 1550-6606 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Alleles Amino Acid Sequence Antigenic determinants, haptens, artificial antigens Antigens Biological and medical sciences Cell Line, Transformed Dynorphins - immunology Epitopes - chemistry Epitopes - immunology Fundamental and applied biological sciences. Psychology Fundamental immunology Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral - immunology HLA-DR Antigens - immunology Humans Molecular immunology Molecular Sequence Data Myoglobin - immunology Peptide Fragments - chemistry Peptide Fragments - immunology Tetanus Toxoid - immunology |
| title | Truncation analysis of several DR binding epitopes |
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