Characterization of the peptide-binding specificity of Mamu-A*11 results in the identification of SIV-derived epitopes and interspecies cross-reactivity
Identifieur interne : 000695 ( Istex/Corpus ); précédent : 000694; suivant : 000696Characterization of the peptide-binding specificity of Mamu-A*11 results in the identification of SIV-derived epitopes and interspecies cross-reactivity
Auteurs : Alessandro Sette ; John Sidney ; Huynh-Hoa Bui ; Marie-France Del Guercio ; Jeff Alexander ; John Loffredo ; David I. Watkins ; Bianca R. MothéSource :
- Immunogenetics [ 0093-7711 ] ; 2005-04-01.
English descriptors
Abstract
Abstract: The SIV-infected Indian rhesus macaque is the most established model of HIV infection, providing insight into pathogenesis and a system for testing novel vaccines. However, only a limited amount of information is available regarding the peptide-binding motifs and epitopes bound by their class I and class II MHC molecules. In this study, we utilized a library of over 1,000 different peptides and a high throughput MHC-peptide binding assay to detail the binding specificity of the rhesus macaque class I molecule Mamu-A*11. These studies defined the fine specificity of primary anchor positions, and dissected the role of secondary anchors, for peptides of 8–11 residues in length. This detailed information was utilized to develop size-specific polynomial algorithms to predict Mamu-A*11 binding capacity. Testing SIVmac239-derived Mamu-A*11 binding peptides for recognition by peripheral blood mononuclear cells (PBMC) from Mamu-A*11-positive, SIV-infected macaques, identified five novel SIV-derived Mamu-A*11 epitopes. Finally, we detected extensive cross-reactivity at the binding level between Mamu-A*11 and the mouse H-2 class I molecule Kk. Further experiments revealed that three out of four Mamu-A*11 binding peptides which bound Kk and were immunogenic in Kk mice were also recognized in Mamu-A*11-infected macaques. This is the first detailed description of mouse-macaque interspecies cross-reactivity, potentially useful in testing novel vaccines in mice and macaques.
Url:
DOI: 10.1007/s00251-004-0749-z
Links to Exploration step
ISTEX:36B40CEB01BD463B7BA2D69A1C78071702798116Le document en format XML
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Watkins</name><affiliation><mods:affiliation>Wisconsin National Primate Research Center, University of Wisconsin-Madison, 53715, Madison, WI, USA</mods:affiliation></affiliation></author><author><name sortKey="Mothe, Bianca R" sort="Mothe, Bianca R" uniqKey="Mothe B" first="Bianca R." last="Mothé">Bianca R. Mothé</name><affiliation><mods:affiliation>Department of Biological Sciences, California State University, San Marcos, 92096, San Marcos, CA, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: bmothe@csusm.edu</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Immunogenetics</title><title level="j" type="abbrev">Immunogenetics</title><idno type="ISSN">0093-7711</idno><idno type="eISSN">1432-1211</idno><imprint><publisher>Springer-Verlag; http://www.springer.de</publisher><pubPlace>Berlin/Heidelberg</pubPlace><date type="published" when="2005-04-01">2005-04-01</date><biblScope unit="volume">57</biblScope><biblScope unit="issue">1-2</biblScope><biblScope unit="page" from="53">53</biblScope><biblScope unit="page" to="68">68</biblScope></imprint><idno type="ISSN">0093-7711</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0093-7711</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>AIDS</term><term>Epitope</term><term>MHC</term><term>Macaque</term><term>SIV</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The SIV-infected Indian rhesus macaque is the most established model of HIV infection, providing insight into pathogenesis and a system for testing novel vaccines. However, only a limited amount of information is available regarding the peptide-binding motifs and epitopes bound by their class I and class II MHC molecules. In this study, we utilized a library of over 1,000 different peptides and a high throughput MHC-peptide binding assay to detail the binding specificity of the rhesus macaque class I molecule Mamu-A*11. These studies defined the fine specificity of primary anchor positions, and dissected the role of secondary anchors, for peptides of 8–11 residues in length. This detailed information was utilized to develop size-specific polynomial algorithms to predict Mamu-A*11 binding capacity. Testing SIVmac239-derived Mamu-A*11 binding peptides for recognition by peripheral blood mononuclear cells (PBMC) from Mamu-A*11-positive, SIV-infected macaques, identified five novel SIV-derived Mamu-A*11 epitopes. Finally, we detected extensive cross-reactivity at the binding level between Mamu-A*11 and the mouse H-2 class I molecule Kk. Further experiments revealed that three out of four Mamu-A*11 binding peptides which bound Kk and were immunogenic in Kk mice were also recognized in Mamu-A*11-infected macaques. This is the first detailed description of mouse-macaque interspecies cross-reactivity, potentially useful in testing novel vaccines in mice and macaques.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Alessandro Sette</name><affiliations><json:string>La Jolla Institute for Allergy and Immunology, 92121, San Diego, CA, USA</json:string></affiliations></json:item><json:item><name>John Sidney</name><affiliations><json:string>La Jolla Institute for Allergy and Immunology, 92121, San Diego, CA, USA</json:string></affiliations></json:item><json:item><name>Huynh-Hoa Bui</name><affiliations><json:string>La Jolla Institute for Allergy and Immunology, 92121, San Diego, CA, USA</json:string></affiliations></json:item><json:item><name>Marie-France del Guercio</name><affiliations><json:string>Epimmune, Inc, 92121, San Diego, CA, USA</json:string></affiliations></json:item><json:item><name>Jeff Alexander</name><affiliations><json:string>Epimmune, Inc, 92121, San Diego, CA, USA</json:string></affiliations></json:item><json:item><name>John Loffredo</name><affiliations><json:string>Wisconsin National Primate Research Center, University of Wisconsin-Madison, 53715, Madison, WI, USA</json:string></affiliations></json:item><json:item><name>David I. Watkins</name><affiliations><json:string>Wisconsin National Primate Research Center, University of Wisconsin-Madison, 53715, Madison, WI, USA</json:string></affiliations></json:item><json:item><name>Bianca R. Mothé</name><affiliations><json:string>Department of Biological Sciences, California State University, San Marcos, 92096, San Marcos, CA, USA</json:string><json:string>E-mail: bmothe@csusm.edu</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>AIDS</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>SIV</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>MHC</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Epitope</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Macaque</value></json:item></subject><articleId><json:string>749</json:string><json:string>Art1</json:string></articleId><arkIstex>ark:/67375/VQC-SPG8817M-3</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: The SIV-infected Indian rhesus macaque is the most established model of HIV infection, providing insight into pathogenesis and a system for testing novel vaccines. However, only a limited amount of information is available regarding the peptide-binding motifs and epitopes bound by their class I and class II MHC molecules. In this study, we utilized a library of over 1,000 different peptides and a high throughput MHC-peptide binding assay to detail the binding specificity of the rhesus macaque class I molecule Mamu-A*11. These studies defined the fine specificity of primary anchor positions, and dissected the role of secondary anchors, for peptides of 8–11 residues in length. This detailed information was utilized to develop size-specific polynomial algorithms to predict Mamu-A*11 binding capacity. Testing SIVmac239-derived Mamu-A*11 binding peptides for recognition by peripheral blood mononuclear cells (PBMC) from Mamu-A*11-positive, SIV-infected macaques, identified five novel SIV-derived Mamu-A*11 epitopes. Finally, we detected extensive cross-reactivity at the binding level between Mamu-A*11 and the mouse H-2 class I molecule Kk. Further experiments revealed that three out of four Mamu-A*11 binding peptides which bound Kk and were immunogenic in Kk mice were also recognized in Mamu-A*11-infected macaques. 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However, only a limited amount of information is available regarding the peptide-binding motifs and epitopes bound by their class I and class II MHC molecules. In this study, we utilized a library of over 1,000 different peptides and a high throughput MHC-peptide binding assay to detail the binding specificity of the rhesus macaque class I molecule Mamu-A*11. These studies defined the fine specificity of primary anchor positions, and dissected the role of secondary anchors, for peptides of 8–11 residues in length. This detailed information was utilized to develop size-specific polynomial algorithms to predict Mamu-A*11 binding capacity. Testing SIVmac239-derived Mamu-A*11 binding peptides for recognition by peripheral blood mononuclear cells (PBMC) from Mamu-A*11-positive, SIV-infected macaques, identified five novel SIV-derived Mamu-A*11 epitopes. Finally, we detected extensive cross-reactivity at the binding level between Mamu-A*11 and the mouse H-2 class I molecule Kk. Further experiments revealed that three out of four Mamu-A*11 binding peptides which bound Kk and were immunogenic in Kk mice were also recognized in Mamu-A*11-infected macaques. This is the first detailed description of mouse-macaque interspecies cross-reactivity, potentially useful in testing novel vaccines in mice and macaques.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>AIDS</term></item><item><term>SIV</term></item><item><term>MHC</term></item><item><term>Epitope</term></item><item><term>Macaque</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2004-09-05">Created</change><change when="2005-04-01">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/VQC-SPG8817M-3/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus springer-journals not found" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType 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DisplayOrder="Western"><GivenName>Alessandro</GivenName><FamilyName>Sette</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>John</GivenName><FamilyName>Sidney</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Huynh-Hoa</GivenName><FamilyName>Bui</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Marie-France</GivenName><Particle>del</Particle><FamilyName>Guercio</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Jeff</GivenName><FamilyName>Alexander</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>John</GivenName><FamilyName>Loffredo</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>David</GivenName><GivenName>I.</GivenName><FamilyName>Watkins</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff4" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Bianca</GivenName><GivenName>R.</GivenName><FamilyName>Mothé</FamilyName></AuthorName><Contact><Phone>+1-760-7503063</Phone><Fax>+1-760-7504637</Fax><Email>bmothe@csusm.edu</Email></Contact></Author><Affiliation ID="Aff1"><OrgName>La Jolla Institute for Allergy and Immunology</OrgName><OrgAddress><City>San Diego</City><State>CA</State><Postcode>92121</Postcode><Country>USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgName>Epimmune, Inc</OrgName><OrgAddress><City>San Diego</City><State>CA</State><Postcode>92121</Postcode><Country>USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgDivision>Wisconsin National Primate Research Center</OrgDivision><OrgName>University of Wisconsin-Madison</OrgName><OrgAddress><City>Madison</City><State>WI</State><Postcode>53715</Postcode><Country>USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff4"><OrgDivision>Department of Biological Sciences</OrgDivision><OrgName>California State University, San Marcos</OrgName><OrgAddress><City>San Marcos</City><State>CA</State><Postcode>92096</Postcode><Country>USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>The SIV-infected Indian rhesus macaque is the most established model of HIV infection, providing insight into pathogenesis and a system for testing novel vaccines. However, only a limited amount of information is available regarding the peptide-binding motifs and epitopes bound by their class I and class II MHC molecules. In this study, we utilized a library of over 1,000 different peptides and a high throughput MHC-peptide binding assay to detail the binding specificity of the rhesus macaque class I molecule Mamu-A*11. These studies defined the fine specificity of primary anchor positions, and dissected the role of secondary anchors, for peptides of 8–11 residues in length. This detailed information was utilized to develop size-specific polynomial algorithms to predict Mamu-A*11 binding capacity. Testing SIV<Subscript>mac</Subscript>239-derived Mamu-A*11 binding peptides for recognition by peripheral blood mononuclear cells (PBMC) from Mamu-A*11-positive, SIV-infected macaques, identified five novel SIV-derived Mamu-A*11 epitopes. Finally, we detected extensive cross-reactivity at the binding level between Mamu-A*11 and the mouse H-2 class I molecule K<Superscript>k</Superscript>. Further experiments revealed that three out of four Mamu-A*11 binding peptides which bound K<Superscript>k</Superscript> and were immunogenic in K<Superscript>k</Superscript> mice were also recognized in Mamu-A*11-infected macaques. This is the first detailed description of mouse-macaque interspecies cross-reactivity, potentially useful in testing novel vaccines in mice and macaques.</Para></Abstract><KeywordGroup Language="En"><Heading>Keywords</Heading><Keyword>AIDS</Keyword><Keyword>SIV</Keyword><Keyword>MHC</Keyword><Keyword>Epitope</Keyword><Keyword>Macaque</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Characterization of the peptide-binding specificity of Mamu-A*11 results in the identification of SIV-derived epitopes and interspecies cross-reactivity</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Characterization of the peptide-binding specificity of Mamu-A*11 results in the identification of SIV-derived epitopes and interspecies cross-reactivity</title></titleInfo><name type="personal"><namePart type="given">Alessandro</namePart><namePart type="family">Sette</namePart><affiliation>La Jolla Institute for Allergy and Immunology, 92121, San Diego, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">John</namePart><namePart type="family">Sidney</namePart><affiliation>La Jolla Institute for Allergy and Immunology, 92121, San Diego, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Huynh-Hoa</namePart><namePart type="family">Bui</namePart><affiliation>La Jolla Institute for Allergy and Immunology, 92121, San Diego, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Marie-France</namePart><namePart type="family">del Guercio</namePart><affiliation>Epimmune, Inc, 92121, San Diego, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jeff</namePart><namePart type="family">Alexander</namePart><affiliation>Epimmune, Inc, 92121, San Diego, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">John</namePart><namePart type="family">Loffredo</namePart><affiliation>Wisconsin National Primate Research Center, University of Wisconsin-Madison, 53715, Madison, WI, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David</namePart><namePart type="given">I.</namePart><namePart type="family">Watkins</namePart><affiliation>Wisconsin National Primate Research Center, University of Wisconsin-Madison, 53715, Madison, WI, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal" displayLabel="corresp"><namePart type="given">Bianca</namePart><namePart type="given">R.</namePart><namePart type="family">Mothé</namePart><affiliation>Department of Biological Sciences, California State University, San Marcos, 92096, San Marcos, CA, USA</affiliation><affiliation>E-mail: bmothe@csusm.edu</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" 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>Springer-Verlag; http://www.springer.de</publisher><place><placeTerm type="text">Berlin/Heidelberg</placeTerm></place><dateCreated encoding="w3cdtf">2004-09-05</dateCreated><dateIssued encoding="w3cdtf">2005-04-01</dateIssued><copyrightDate encoding="w3cdtf">2005</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: The SIV-infected Indian rhesus macaque is the most established model of HIV infection, providing insight into pathogenesis and a system for testing novel vaccines. However, only a limited amount of information is available regarding the peptide-binding motifs and epitopes bound by their class I and class II MHC molecules. In this study, we utilized a library of over 1,000 different peptides and a high throughput MHC-peptide binding assay to detail the binding specificity of the rhesus macaque class I molecule Mamu-A*11. These studies defined the fine specificity of primary anchor positions, and dissected the role of secondary anchors, for peptides of 8–11 residues in length. This detailed information was utilized to develop size-specific polynomial algorithms to predict Mamu-A*11 binding capacity. Testing SIVmac239-derived Mamu-A*11 binding peptides for recognition by peripheral blood mononuclear cells (PBMC) from Mamu-A*11-positive, SIV-infected macaques, identified five novel SIV-derived Mamu-A*11 epitopes. Finally, we detected extensive cross-reactivity at the binding level between Mamu-A*11 and the mouse H-2 class I molecule Kk. Further experiments revealed that three out of four Mamu-A*11 binding peptides which bound Kk and were immunogenic in Kk mice were also recognized in Mamu-A*11-infected macaques. This is the first detailed description of mouse-macaque interspecies cross-reactivity, potentially useful in testing novel vaccines in mice and macaques.</abstract><note>Original Paper</note><subject lang="en"><genre>Keywords</genre><topic>AIDS</topic><topic>SIV</topic><topic>MHC</topic><topic>Epitope</topic><topic>Macaque</topic></subject><relatedItem type="host"><titleInfo><title>Immunogenetics</title></titleInfo><titleInfo type="abbreviated"><title>Immunogenetics</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>Springer</publisher><dateIssued encoding="w3cdtf">2005-04-16</dateIssued><copyrightDate encoding="w3cdtf">2005</copyrightDate></originInfo><subject><genre>LifeSciences</genre></subject><identifier type="ISSN">0093-7711</identifier><identifier type="eISSN">1432-1211</identifier><identifier type="JournalID">251</identifier><part><date>2005</date><detail type="volume"><number>57</number><caption>vol.</caption></detail><detail type="issue"><number>1-2</number><caption>no.</caption></detail><extent unit="pages"><start>53</start><end>68</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 2005</recordOrigin></recordInfo></relatedItem><identifier type="istex">36B40CEB01BD463B7BA2D69A1C78071702798116</identifier><identifier type="ark">ark:/67375/VQC-SPG8817M-3</identifier><identifier type="DOI">10.1007/s00251-004-0749-z</identifier><identifier type="ArticleID">749</identifier><identifier type="ArticleID">Art1</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 2005</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Springer-Verlag, 2005</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-SPG8817M-3/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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