HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes
Identifieur interne : 000822 ( Istex/Corpus ); précédent : 000821; suivant : 000823HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes
Auteurs : Xin-Ting Fu ; Robert W. KarrSource :
- Human Immunology [ 0198-8859 ] ; 1994.
English descriptors
- Teeft :
- Andrea sant, Cdna, Cell line, Chain residues, Cham, Channel fluorescence, Clone, Crystal structure, Direct contact, Drot, Drot chain, Drot cham, Drot residues, Epitope, Epltopes, Expressmn vector, Groove, Heddy zola, Human class, Hybrid molecules, Immunol, Karr, Lechler, Less hkely, Mabs, Molecule, Molecules implications, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Mutant, Outer loops, Outer surface, Polymorphic, Polymorphic chain residues, Polymorphlc, Residue, Robert lechler, Sanna goyert, Several residues, Side chain, Soldano ferrone, Stefan carrel, Superantlgen binding, Toxin, Transfectants.
Abstract
Abstract: The structure-function relationships of the HLA-DRα chain have been analyzed by identifying DRα residues involved in several nonpolymorphic and polymorphic antibody epitopes. Antibody binding to transfectants expressing a WT or mutant DRα chain with the WT DR (β1∗0701) chain was analyzed. Our results indicate that residues 18, 36, and 39 located on the outer loops of the DRα chain are critical for one of more of the epitopes recognized by the SG157, Q2/70, L243, LB3. 1, D1-12, and CL413 mAbs. Similar results were obtained when the DRα position 18 and 39 mutants were expressed with other DRβ1 allesles. Furthermore, residues 15 and 18 of the DRα chain were shown to be involved in the epitopes of two polymorphic mAbs, HU-26 and I-2, whose epitopes also include residue 4 of the corresponding DRβ chains. In addition to their involvement in antibody-binding epitopes, residues in this region on the outer surface of the DRα chain have also been shown to be involved in superantigen binding and presentation and T-cell recognition of foreign antigen, emphasizing the functional importance of DRα-chain residues located outside of the peptide-binding groove.
Url:
DOI: 10.1016/0198-8859(94)90268-2
Links to Exploration step
ISTEX:23A1B868EC5B00236B6C5A8147FC1A0CDE71861BLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes</title><author><name sortKey="Fu, Xin Ting" sort="Fu, Xin Ting" uniqKey="Fu X" first="Xin-Ting" last="Fu">Xin-Ting Fu</name><affiliation><mods:affiliation>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</mods:affiliation></affiliation></author><author><name sortKey="Karr, Robert W" sort="Karr, Robert W" uniqKey="Karr R" first="Robert W." last="Karr">Robert W. Karr</name><affiliation><mods:affiliation>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:23A1B868EC5B00236B6C5A8147FC1A0CDE71861B</idno><date when="1994" year="1994">1994</date><idno type="doi">10.1016/0198-8859(94)90268-2</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-6ZDHT1TW-3/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000822</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000822</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes</title><author><name sortKey="Fu, Xin Ting" sort="Fu, Xin Ting" uniqKey="Fu X" first="Xin-Ting" last="Fu">Xin-Ting Fu</name><affiliation><mods:affiliation>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</mods:affiliation></affiliation></author><author><name sortKey="Karr, Robert W" sort="Karr, Robert W" uniqKey="Karr R" first="Robert W." last="Karr">Robert W. Karr</name><affiliation><mods:affiliation>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Human Immunology</title><title level="j" type="abbrev">HIM</title><idno type="ISSN">0198-8859</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">39</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="253">253</biblScope><biblScope unit="page" to="260">260</biblScope></imprint><idno type="ISSN">0198-8859</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0198-8859</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Andrea sant</term><term>Cdna</term><term>Cell line</term><term>Chain residues</term><term>Cham</term><term>Channel fluorescence</term><term>Clone</term><term>Crystal structure</term><term>Direct contact</term><term>Drot</term><term>Drot chain</term><term>Drot cham</term><term>Drot residues</term><term>Epitope</term><term>Epltopes</term><term>Expressmn vector</term><term>Groove</term><term>Heddy zola</term><term>Human class</term><term>Hybrid molecules</term><term>Immunol</term><term>Karr</term><term>Lechler</term><term>Less hkely</term><term>Mabs</term><term>Molecule</term><term>Molecules implications</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Mutant</term><term>Outer loops</term><term>Outer surface</term><term>Polymorphic</term><term>Polymorphic chain residues</term><term>Polymorphlc</term><term>Residue</term><term>Robert lechler</term><term>Sanna goyert</term><term>Several residues</term><term>Side chain</term><term>Soldano ferrone</term><term>Stefan carrel</term><term>Superantlgen binding</term><term>Toxin</term><term>Transfectants</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The structure-function relationships of the HLA-DRα chain have been analyzed by identifying DRα residues involved in several nonpolymorphic and polymorphic antibody epitopes. Antibody binding to transfectants expressing a WT or mutant DRα chain with the WT DR (β1∗0701) chain was analyzed. Our results indicate that residues 18, 36, and 39 located on the outer loops of the DRα chain are critical for one of more of the epitopes recognized by the SG157, Q2/70, L243, LB3. 1, D1-12, and CL413 mAbs. Similar results were obtained when the DRα position 18 and 39 mutants were expressed with other DRβ1 allesles. Furthermore, residues 15 and 18 of the DRα chain were shown to be involved in the epitopes of two polymorphic mAbs, HU-26 and I-2, whose epitopes also include residue 4 of the corresponding DRβ chains. In addition to their involvement in antibody-binding epitopes, residues in this region on the outer surface of the DRα chain have also been shown to be involved in superantigen binding and presentation and T-cell recognition of foreign antigen, emphasizing the functional importance of DRα-chain residues located outside of the peptide-binding groove.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>immunol</json:string><json:string>drot</json:string><json:string>epltopes</json:string><json:string>mabs</json:string><json:string>mutant</json:string><json:string>epitope</json:string><json:string>karr</json:string><json:string>cham</json:string><json:string>transfectants</json:string><json:string>monoclonal</json:string><json:string>polymorphlc</json:string><json:string>outer loops</json:string><json:string>cdna</json:string><json:string>lechler</json:string><json:string>polymorphic</json:string><json:string>clone</json:string><json:string>monoclonal antibody</json:string><json:string>drot chain</json:string><json:string>crystal structure</json:string><json:string>monoclonal antibodies</json:string><json:string>chain residues</json:string><json:string>molecule</json:string><json:string>residue</json:string><json:string>toxin</json:string><json:string>groove</json:string><json:string>hybrid molecules</json:string><json:string>expressmn vector</json:string><json:string>andrea sant</json:string><json:string>superantlgen binding</json:string><json:string>robert lechler</json:string><json:string>heddy zola</json:string><json:string>sanna goyert</json:string><json:string>stefan carrel</json:string><json:string>soldano ferrone</json:string><json:string>human class</json:string><json:string>drot cham</json:string><json:string>outer surface</json:string><json:string>less hkely</json:string><json:string>several residues</json:string><json:string>direct contact</json:string><json:string>side chain</json:string><json:string>channel fluorescence</json:string><json:string>polymorphic chain residues</json:string><json:string>drot residues</json:string><json:string>cell line</json:string><json:string>molecules implications</json:string></teeft></keywords><author><json:item><name>Xin-Ting Fu</name><affiliations><json:string>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</json:string></affiliations></json:item><json:item><name>Robert W. Karr</name><affiliations><json:string>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-6ZDHT1TW-3</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The structure-function relationships of the HLA-DRα chain have been analyzed by identifying DRα residues involved in several nonpolymorphic and polymorphic antibody epitopes. Antibody binding to transfectants expressing a WT or mutant DRα chain with the WT DR (β1∗0701) chain was analyzed. Our results indicate that residues 18, 36, and 39 located on the outer loops of the DRα chain are critical for one of more of the epitopes recognized by the SG157, Q2/70, L243, LB3. 1, D1-12, and CL413 mAbs. Similar results were obtained when the DRα position 18 and 39 mutants were expressed with other DRβ1 allesles. Furthermore, residues 15 and 18 of the DRα chain were shown to be involved in the epitopes of two polymorphic mAbs, HU-26 and I-2, whose epitopes also include residue 4 of the corresponding DRβ chains. In addition to their involvement in antibody-binding epitopes, residues in this region on the outer surface of the DRα chain have also been shown to be involved in superantigen binding and presentation and T-cell recognition of foreign antigen, emphasizing the functional importance of DRα-chain residues located outside of the peptide-binding groove.</abstract><qualityIndicators><score>9.22</score><pdfWordCount>6023</pdfWordCount><pdfCharCount>29563</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>562 x 778 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>185</abstractWordCount><abstractCharCount>1172</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes</title><pmid><json:string>7520896</json:string></pmid><pii><json:string>0198-8859(94)90268-2</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc Natl Acad Sci USA</title><language><json:string>unknown</json:string></language><volume>87</volume><pages><first>8051</first></pages></serie><host><title>Human Immunology</title><language><json:string>unknown</json:string></language><publicationDate>1994</publicationDate><issn><json:string>0198-8859</json:string></issn><pii><json:string>S0198-8859(00)X0221-2</json:string></pii><volume>39</volume><issue>4</issue><pages><first>253</first><last>260</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>44S</json:string><json:string>14-4-4</json:string><json:string>1994</json:string></date><geogName><json:string>Sanna</json:string></geogName><orgName><json:string>Monsanto Co</json:string><json:string>American Type Culture Collection, Rockvmlle, MD, USA</json:string><json:string>American Type Culture Collectmn</json:string><json:string>Cancer Research, Epahnges, Swltzerland</json:string><json:string>University of Chicago</json:string><json:string>Western General Hospital, Edmburgh, Scotland</json:string><json:string>National Institutes of Health</json:string></orgName><orgName_funder><json:string>National Institutes of Health</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Ludwig Insntute</json:string><json:string>Peter Gregersen</json:string><json:string>Robert Lechler</json:string><json:string>Is</json:string><json:string>Stefan Carrel</json:string><json:string>Proc Natl</json:string><json:string>Heddy Zola</json:string><json:string>Lechler</json:string><json:string>Andrea Sant</json:string><json:string>Jack Strominger</json:string><json:string>Thls</json:string><json:string>Dan Larhammar</json:string><json:string>Akemi Wakisaka</json:string><json:string>Jim Miller</json:string><json:string>Barber</json:string><json:string>Jack Stromlnger</json:string><json:string>Jerry Brown</json:string></persName><placeName><json:string>Bedford</json:string><json:string>IL</json:string><json:string>San Diego</json:string><json:string>UK</json:string><json:string>London</json:string><json:string>USA</json:string><json:string>Japan</json:string><json:string>Chicago</json:string><json:string>CA</json:string><json:string>York</json:string><json:string>MA</json:string><json:string>Cambridge</json:string><json:string>Sweden</json:string><json:string>Sapporo</json:string><json:string>Mountain View</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[50]</json:string><json:string>[4]</json:string><json:string>[34]</json:string><json:string>Fu et al</json:string><json:string>[29]</json:string><json:string>[33]</json:string><json:string>[1-7]</json:string><json:string>[8]</json:string><json:string>[39]</json:string><json:string>[54]</json:string><json:string>[48, 49]</json:string><json:string>Nygard et al</json:string><json:string>[43-45]</json:string><json:string>[37]</json:string><json:string>[ 19]</json:string><json:string>[41]</json:string><json:string>[47]</json:string><json:string>[40]</json:string><json:string>[5, 38]</json:string><json:string>[ 1-7]</json:string><json:string>[46]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-6ZDHT1TW-3</json:string></ark><categories><wos><json:string>1 - 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Fu, Monsanto Co./AA4C, 700 Chesterfield Parkway North, St. Louis, MO 63198, USA</note><affiliation>Address reprint requests to Dr. X.-T. Fu, Monsanto Co./AA4C, 700 Chesterfield Parkway North, St. Louis, MO 63198, USA</affiliation><affiliation>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Robert W.</forename><surname>Karr</surname></persName><affiliation>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</affiliation></author><idno type="istex">23A1B868EC5B00236B6C5A8147FC1A0CDE71861B</idno><idno type="ark">ark:/67375/6H6-6ZDHT1TW-3</idno><idno type="DOI">10.1016/0198-8859(94)90268-2</idno><idno type="PII">0198-8859(94)90268-2</idno></analytic><monogr><title level="j">Human Immunology</title><title level="j" type="abbrev">HIM</title><idno type="pISSN">0198-8859</idno><idno type="PII">S0198-8859(00)X0221-2</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994"></date><biblScope unit="volume">39</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="253">253</biblScope><biblScope unit="page" to="260">260</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1994</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The structure-function relationships of the HLA-DRα chain have been analyzed by identifying DRα residues involved in several nonpolymorphic and polymorphic antibody epitopes. Antibody binding to transfectants expressing a WT or mutant DRα chain with the WT DR (β1∗0701) chain was analyzed. Our results indicate that residues 18, 36, and 39 located on the outer loops of the DRα chain are critical for one of more of the epitopes recognized by the SG157, Q2/70, L243, LB3. 1, D1-12, and CL413 mAbs. Similar results were obtained when the DRα position 18 and 39 mutants were expressed with other DRβ1 allesles. Furthermore, residues 15 and 18 of the DRα chain were shown to be involved in the epitopes of two polymorphic mAbs, HU-26 and I-2, whose epitopes also include residue 4 of the corresponding DRβ chains. In addition to their involvement in antibody-binding epitopes, residues in this region on the outer surface of the DRα chain have also been shown to be involved in superantigen binding and presentation and T-cell recognition of foreign antigen, emphasizing the functional importance of DRα-chain residues located outside of the peptide-binding groove.</p></abstract></profileDesc><revisionDesc><change when="1994">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-6ZDHT1TW-3/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>HIM</jid><aid>94902682</aid><ce:pii>0198-8859(94)90268-2</ce:pii><ce:doi>10.1016/0198-8859(94)90268-2</ce:doi><ce:copyright type="unknown" year="1994"></ce:copyright></item-info><head><ce:title>HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes</ce:title><ce:author-group><ce:author><ce:given-name>Xin-Ting</ce:given-name><ce:surname>Fu</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Robert W.</ce:given-name><ce:surname>Karr</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Address reprint requests to Dr. X.-T. Fu, Monsanto Co./AA4C, 700 Chesterfield Parkway North, St. Louis, MO 63198, USA</ce:text></ce:correspondence></ce:author-group><ce:date-received day="28" month="6" year="1993"></ce:date-received><ce:date-accepted day="8" month="10" year="1993"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The structure-function relationships of the HLA-DRα chain have been analyzed by identifying DRα residues involved in several nonpolymorphic and polymorphic antibody epitopes. Antibody binding to transfectants expressing a WT or mutant DRα chain with the WT DR (β1<ce:sup>∗</ce:sup>0701) chain was analyzed. Our results indicate that residues 18, 36, and 39 located on the outer loops of the DRα chain are critical for one of more of the epitopes recognized by the SG157, Q2/70, L243, LB3. 1, D1-12, and CL413 mAbs. Similar results were obtained when the DRα position 18 and 39 mutants were expressed with other DRβ1 allesles. Furthermore, residues 15 and 18 of the DRα chain were shown to be involved in the epitopes of two polymorphic mAbs, HU-26 and I-2, whose epitopes also include residue 4 of the corresponding DRβ chains. In addition to their involvement in antibody-binding epitopes, residues in this region on the outer surface of the DRα chain have also been shown to be involved in superantigen binding and presentation and T-cell recognition of foreign antigen, emphasizing the functional importance of DRα-chain residues located outside of the peptide-binding groove.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes</title></titleInfo><name type="personal"><namePart type="given">Xin-Ting</namePart><namePart type="family">Fu</namePart><affiliation>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</affiliation><description>Address reprint requests to Dr. X.-T. Fu, Monsanto Co./AA4C, 700 Chesterfield Parkway North, St. Louis, MO 63198, USA</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Robert W.</namePart><namePart type="family">Karr</namePart><affiliation>Department of Immunology and Infectious Diseases, Monsanto Company, St. Louis, Missouri, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1994</dateIssued><copyrightDate encoding="w3cdtf">1994</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The structure-function relationships of the HLA-DRα chain have been analyzed by identifying DRα residues involved in several nonpolymorphic and polymorphic antibody epitopes. Antibody binding to transfectants expressing a WT or mutant DRα chain with the WT DR (β1∗0701) chain was analyzed. Our results indicate that residues 18, 36, and 39 located on the outer loops of the DRα chain are critical for one of more of the epitopes recognized by the SG157, Q2/70, L243, LB3. 1, D1-12, and CL413 mAbs. Similar results were obtained when the DRα position 18 and 39 mutants were expressed with other DRβ1 allesles. Furthermore, residues 15 and 18 of the DRα chain were shown to be involved in the epitopes of two polymorphic mAbs, HU-26 and I-2, whose epitopes also include residue 4 of the corresponding DRβ chains. In addition to their involvement in antibody-binding epitopes, residues in this region on the outer surface of the DRα chain have also been shown to be involved in superantigen binding and presentation and T-cell recognition of foreign antigen, emphasizing the functional importance of DRα-chain residues located outside of the peptide-binding groove.</abstract><relatedItem type="host"><titleInfo><title>Human Immunology</title></titleInfo><titleInfo type="abbreviated"><title>HIM</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1994</dateIssued></originInfo><identifier type="ISSN">0198-8859</identifier><identifier type="PII">S0198-8859(00)X0221-2</identifier><part><date>1994</date><detail type="volume"><number>39</number><caption>vol.</caption></detail><detail type="issue"><number>4</number><caption>no.</caption></detail><extent unit="issue-pages"><start>233</start><end>302</end></extent><extent unit="pages"><start>253</start><end>260</end></extent></part></relatedItem><identifier type="istex">23A1B868EC5B00236B6C5A8147FC1A0CDE71861B</identifier><identifier type="ark">ark:/67375/6H6-6ZDHT1TW-3</identifier><identifier type="DOI">10.1016/0198-8859(94)90268-2</identifier><identifier type="PII">0198-8859(94)90268-2</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-6ZDHT1TW-3/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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