Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein
Identifieur interne : 000888 ( Istex/Corpus ); précédent : 000887; suivant : 000889Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein
Auteurs : Kai W. Wucherpfennig ; Jack L. StromingerSource :
- Cell [ 0092-8674 ] ; 1995.
English descriptors
- Teeft :
- Adenovirus, Aliphatic, Allogeneic feeder cells, Amino, Amino acids, Antigenic, Aromatic residues, Aspartic acid, Autoimmunity, Autoreactive, Bacterial peptides, Cell activation, Cell clone, Cell clones, Cell epitope, Cell epitopes, Cell line, Cell lines, Cell proliferation, Cell receptor, Cell recognition, Cell response, Cell stimulation, Cerebrospinal fluid, Clonal, Clonal expansion, Clone, Contact residues, Cytomegalovirus, Drb1, Epitope, Hemagglutinin, Herpes, Herpes simplex, Immunodominant, Immunodominant myelin, Immunodominant peptide, Immunol, Influenza, Influenza type, Lymphocyte, Lytic cycle, Mimicry, Mimicry epitopes, Mimicry peptide, Mimicry peptides, Molecular mimicry, Multiple sclerosis, Multiple sclerosis patients, Mutational analysis, Myelin, Papillomavirus, Pathogen, Peptide, Peptide conformation, Phorbol, Polymerase, Positive control, Protein peptide, Pseudomonas, Sclerosis, Search criteria, Simplex, Stimulatory, Stimulatory capacity, Structural requirements, Substitution, Subtypes, Viral, Viral mimicry peptides, Viral peptides, Wucherpfennig.
Abstract
Abstract: Structural similarity between viral T cell epitopes and self-peptides could lead to the induction of an autoaggressive T cell response. Based on the structural requirements for both MHC class 11 binding and TCR recognition of an immunodominant myelin basic protein (MBP) peptide, criteria for a data base search were developed in which the degeneracy of amino acid side chains required for MHC class 11 binding and the conservation of those required for T cell activation were considered. A panel of 129 peptides that matched the molecular mimicry motif was tested on seven MBP-specific T cell clones from multiple sclerosis patients. Seven viral and one bacterial peptide efficiently activated three of these clones. Only one peptide could have been identified as a molecular mimic by sequence alignment. The observation that a single T cell receptor can recognize quite distinct but structurally related peptides from multiple pathogens has important implications for understanding the pathogenesis of autoimmunity.
Url:
DOI: 10.1016/0092-8674(95)90348-8
Links to Exploration step
ISTEX:B1572F523C527B4C00D93E43B7B100F47D61DEA0Le document en format XML
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Based on the structural requirements for both MHC class 11 binding and TCR recognition of an immunodominant myelin basic protein (MBP) peptide, criteria for a data base search were developed in which the degeneracy of amino acid side chains required for MHC class 11 binding and the conservation of those required for T cell activation were considered. A panel of 129 peptides that matched the molecular mimicry motif was tested on seven MBP-specific T cell clones from multiple sclerosis patients. Seven viral and one bacterial peptide efficiently activated three of these clones. Only one peptide could have been identified as a molecular mimic by sequence alignment. 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Based on the structural requirements for both MHC class 11 binding and TCR recognition of an immunodominant myelin basic protein (MBP) peptide, criteria for a data base search were developed in which the degeneracy of amino acid side chains required for MHC class 11 binding and the conservation of those required for T cell activation were considered. A panel of 129 peptides that matched the molecular mimicry motif was tested on seven MBP-specific T cell clones from multiple sclerosis patients. Seven viral and one bacterial peptide efficiently activated three of these clones. Only one peptide could have been identified as a molecular mimic by sequence alignment. The observation that a single T cell receptor can recognize quite distinct but structurally related peptides from multiple pathogens has important implications for understanding the pathogenesis of autoimmunity.</abstract><qualityIndicators><score>8.86</score><pdfWordCount>7869</pdfWordCount><pdfCharCount>52906</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>612 x 828 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>155</abstractWordCount><abstractCharCount>1027</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein</title><pmid><json:string>7534214</json:string></pmid><pii><json:string>0092-8674(95)90348-8</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Handbook of Clinical Neurology</title><language><json:string>unknown</json:string></language><pages><first>259</first><last>287</last></pages><editor><json:item><name>P.J Vinken</name></json:item><json:item><name>G.W Bruyn</name></json:item><json:item><name>H.L Klawans</name></json:item><json:item><name>J.C Koetsier</name></json:item></editor></serie><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1995</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0615-0</json:string></pii><volume>80</volume><issue>5</issue><pages><first>695</first><last>705</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>10s</json:string><json:string>1995</json:string></date><geogName></geogName><orgName><json:string>O CO</json:string><json:string>National Multiple Sclerosis Society</json:string><json:string>Harvard University</json:string><json:string>Murex Diagnostics, Dartford, England</json:string><json:string>National Multiple Sclerosis Society</json:string><json:string>CA</json:string><json:string>National Institutes of Health</json:string></orgName><orgName_funder><json:string>National Multiple Sclerosis Society</json:string><json:string>CA</json:string><json:string>National Institutes of Health</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Kai W. Wucherpfennig</json:string><json:string>Results Structural</json:string><json:string>Ob</json:string><json:string>Viral Epitopes</json:string><json:string>K. Falk</json:string><json:string>Viral Peptides</json:string><json:string>Hy</json:string><json:string>Mike Farzan</json:string><json:string>David Hafler</json:string><json:string>Jack</json:string><json:string>Recent</json:string><json:string>Anne L. Wucherpfennig</json:string><json:string>Viral Variants</json:string><json:string>Scholar</json:string></persName><placeName><json:string>Bedford</json:string><json:string>San Diego</json:string><json:string>SY</json:string><json:string>Mannheim</json:string><json:string>MA</json:string><json:string>Capacity</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Datta et al., 1980</json:string><json:string>Oldstone, 1990</json:string><json:string>Ota et al., 1990</json:string><json:string>Sebzda et al., 1994</json:string><json:string>Brown et al., 1993</json:string><json:string>Martin et al., 1990</json:string><json:string>reviewed by Zamvil and Steinman, 1990</json:string><json:string>Madden et al., 1993</json:string><json:string>Schluesener and Wekerle, 1985</json:string><json:string>Allegretta et al., 1990</json:string><json:string>Fujinami and Oldstone, 1985</json:string><json:string>Wucherpfennig et al., 1994b</json:string><json:string>Zhang et al., 1994</json:string><json:string>Friedman et al., 1991</json:string><json:string>Baig et al., 1989</json:string><json:string>Brocke et al., 1993</json:string><json:string>Kisielow et al., 1988</json:string><json:string>Burns et al., 1983</json:string><json:string>Kurtzke, 1985</json:string><json:string>Conrad et al., 1994</json:string><json:string>Chambers et al., 1989</json:string><json:string>Pette et al., 1990</json:string><json:string>Wucherpfennig et al., 1994a</json:string><json:string>Brown et al., 1991</json:string><json:string>Wucherpfennig et al., 1994a, 1994b</json:string><json:string>Spielman and Nathenson, 1982</json:string><json:string>Johnson et al., 1984</json:string><json:string>Rose et al., 1986</json:string><json:string>Ofa et aL, 1990</json:string><json:string>Stadt et al., 1990</json:string><json:string>Tisch et al., 1993</json:string><json:string>Reay et al., 1994</json:string><json:string>Lehmann et al., 1992</json:string><json:string>Kurtzke and Hyllestad, 1979</json:string><json:string>Hickey et al., 1991</json:string><json:string>Vogt et al., 1994</json:string><json:string>Cole and Griffiths, 1993</json:string><json:string>Burrows et al., 1994</json:string><json:string>Ray et al., 1980</json:string><json:string>Kaufman et al., 1993</json:string><json:string>Olerup et al., 1989</json:string><json:string>van Eden et al., 1985, 1988</json:string><json:string>Busch et al., 1991</json:string><json:string>Wekerie et al., 1986</json:string><json:string>Wucherpfennig et al., 1991</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-5S07CK3V-D</json:string></ark><categories><wos><json:string>1 - 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Based on the structural requirements for both MHC class 11 binding and TCR recognition of an immunodominant myelin basic protein (MBP) peptide, criteria for a data base search were developed in which the degeneracy of amino acid side chains required for MHC class 11 binding and the conservation of those required for T cell activation were considered. A panel of 129 peptides that matched the molecular mimicry motif was tested on seven MBP-specific T cell clones from multiple sclerosis patients. Seven viral and one bacterial peptide efficiently activated three of these clones. Only one peptide could have been identified as a molecular mimic by sequence alignment. The observation that a single T cell receptor can recognize quite distinct but structurally related peptides from multiple pathogens has important implications for understanding the pathogenesis of autoimmunity.</p></abstract></profileDesc><revisionDesc><change when="1994-12-15">Modified</change><change when="1995">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-5S07CK3V-D/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>CELL</jid><aid>95903488</aid><ce:pii>0092-8674(95)90348-8</ce:pii><ce:doi>10.1016/0092-8674(95)90348-8</ce:doi><ce:copyright type="unknown" year="1995"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein</ce:title><ce:author-group><ce:author><ce:given-name>Kai W</ce:given-name><ce:surname>Wucherpfennig</ce:surname></ce:author><ce:author><ce:given-name>Jack L</ce:given-name><ce:surname>Strominger</ce:surname></ce:author><ce:affiliation><ce:textfn>Department of Molecular and Cellular Biology Harvard University Cambridge, Massachusetts, 02138, USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="15" month="11" year="1994"></ce:date-received><ce:date-revised day="15" month="12" year="1994"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Structural similarity between viral T cell epitopes and self-peptides could lead to the induction of an autoaggressive T cell response. Based on the structural requirements for both MHC class 11 binding and TCR recognition of an immunodominant myelin basic protein (MBP) peptide, criteria for a data base search were developed in which the degeneracy of amino acid side chains required for MHC class 11 binding and the conservation of those required for T cell activation were considered. A panel of 129 peptides that matched the molecular mimicry motif was tested on seven MBP-specific T cell clones from multiple sclerosis patients. Seven viral and one bacterial peptide efficiently activated three of these clones. Only one peptide could have been identified as a molecular mimic by sequence alignment. The observation that a single T cell receptor can recognize quite distinct but structurally related peptides from multiple pathogens has important implications for understanding the pathogenesis of autoimmunity.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Molecular mimicry in T cell-mediated autoimmunity: Viral peptides activate human T cell clones specific for myelin basic protein</title></titleInfo><name type="personal"><namePart type="given">Kai W</namePart><namePart type="family">Wucherpfennig</namePart><affiliation>Department of Molecular and Cellular Biology Harvard University Cambridge, Massachusetts, 02138, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jack L</namePart><namePart type="family">Strominger</namePart><affiliation>Department of Molecular and Cellular Biology Harvard University Cambridge, Massachusetts, 02138, 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">1995</dateIssued><dateModified encoding="w3cdtf">1994-12-15</dateModified><copyrightDate encoding="w3cdtf">1995</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Structural similarity between viral T cell epitopes and self-peptides could lead to the induction of an autoaggressive T cell response. Based on the structural requirements for both MHC class 11 binding and TCR recognition of an immunodominant myelin basic protein (MBP) peptide, criteria for a data base search were developed in which the degeneracy of amino acid side chains required for MHC class 11 binding and the conservation of those required for T cell activation were considered. A panel of 129 peptides that matched the molecular mimicry motif was tested on seven MBP-specific T cell clones from multiple sclerosis patients. Seven viral and one bacterial peptide efficiently activated three of these clones. Only one peptide could have been identified as a molecular mimic by sequence alignment. The observation that a single T cell receptor can recognize quite distinct but structurally related peptides from multiple pathogens has important implications for understanding the pathogenesis of autoimmunity.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</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">1995</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0615-0</identifier><part><date>1995</date><detail type="volume"><number>80</number><caption>vol.</caption></detail><detail type="issue"><number>5</number><caption>no.</caption></detail><extent unit="issue-pages"><start>671</start><end>823</end></extent><extent unit="pages"><start>695</start><end>705</end></extent></part></relatedItem><identifier type="istex">B1572F523C527B4C00D93E43B7B100F47D61DEA0</identifier><identifier type="ark">ark:/67375/6H6-5S07CK3V-D</identifier><identifier type="DOI">10.1016/0092-8674(95)90348-8</identifier><identifier type="PII">0092-8674(95)90348-8</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:/67375/6H6-5S07CK3V-D/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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