CTL recognition of a novel HLA-A*0201-binding peptide derived from glioblastoma multiforme tumor cells
Identifieur interne : 000197 ( Istex/Corpus ); précédent : 000196; suivant : 000198CTL recognition of a novel HLA-A*0201-binding peptide derived from glioblastoma multiforme tumor cells
Auteurs : Cheryl E. Myers ; Paul Hanavan ; Kwasi Antwi ; Daruka Mahadevan ; A. Jamal Nadeem ; Laurence Cooke ; Adrienne C. Scheck ; Zachary Laughrey ; Douglas F. LakeSource :
- Cancer Immunology, Immunotherapy [ 0340-7004 ] ; 2011-09-01.
English descriptors
Abstract
Abstract: Genetic instability of tumor cells can result in translation of proteins that are out of frame, resulting in expression of neopeptides. These neopeptides are not self-proteins and therefore should be immunogenic. By eluting peptides from human glioblastoma multiforme (GBM) tumor cell surfaces and subjecting them to tandem mass spectrometry, we identified a novel peptide (KLWGLTPKVTPS) corresponding to a frameshift in the 3′ beta-hydroxysteroid dehydrogenase type 7 (HSD3B7) gene. HLA-binding algorithms predicted that a 9-amino acid sequence embedded in this peptide would bind to HLA-A*0201. We confirmed this prediction using an HLA-A*0201 refolding assay followed by live cell relative affinity assays, but also showed that the 12-mer binds to HLA-A*0201. Based on the 9-mer sequence, optimized peptide ligands (OPL) were designed and tested for their affinities to HLA-A*0201 and their abilities to elicit anti-peptide and CTL capable of killing GBM in vitro. Wild-type peptides as well as OPL induced anti-peptide CTL as measured by IFN-γ ELISPOTS. These CTL also killed GBM tumor cells in chromium-51 release assays. This study reports a new CTL target in GBM and further substantiates the concept that rational design and testing of multiple peptides for the same T-cell epitope elicits a broader response among different individuals than single peptide immunization.
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DOI: 10.1007/s00262-011-1032-4
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These neopeptides are not self-proteins and therefore should be immunogenic. By eluting peptides from human glioblastoma multiforme (GBM) tumor cell surfaces and subjecting them to tandem mass spectrometry, we identified a novel peptide (KLWGLTPKVTPS) corresponding to a frameshift in the 3′ beta-hydroxysteroid dehydrogenase type 7 (HSD3B7) gene. HLA-binding algorithms predicted that a 9-amino acid sequence embedded in this peptide would bind to HLA-A*0201. We confirmed this prediction using an HLA-A*0201 refolding assay followed by live cell relative affinity assays, but also showed that the 12-mer binds to HLA-A*0201. Based on the 9-mer sequence, optimized peptide ligands (OPL) were designed and tested for their affinities to HLA-A*0201 and their abilities to elicit anti-peptide and CTL capable of killing GBM in vitro. Wild-type peptides as well as OPL induced anti-peptide CTL as measured by IFN-γ ELISPOTS. These CTL also killed GBM tumor cells in chromium-51 release assays. 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These neopeptides are not self-proteins and therefore should be immunogenic. By eluting peptides from human glioblastoma multiforme (GBM) tumor cell surfaces and subjecting them to tandem mass spectrometry, we identified a novel peptide (KLWGLTPKVTPS) corresponding to a frameshift in the 3′ beta-hydroxysteroid dehydrogenase type 7 (HSD3B7) gene. HLA-binding algorithms predicted that a 9-amino acid sequence embedded in this peptide would bind to HLA-A*0201. We confirmed this prediction using an HLA-A*0201 refolding assay followed by live cell relative affinity assays, but also showed that the 12-mer binds to HLA-A*0201. Based on the 9-mer sequence, optimized peptide ligands (OPL) were designed and tested for their affinities to HLA-A*0201 and their abilities to elicit anti-peptide and CTL capable of killing GBM in vitro. Wild-type peptides as well as OPL induced anti-peptide CTL as measured by IFN-γ ELISPOTS. These CTL also killed GBM tumor cells in chromium-51 release assays. 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article</ArticleCategory><ArticleFirstPage>1319</ArticleFirstPage><ArticleLastPage>1332</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2011</Year><Month>5</Month><Day>10</Day></RegistrationDate><Received><Year>2010</Year><Month>3</Month><Day>24</Day></Received><Accepted><Year>2011</Year><Month>5</Month><Day>9</Day></Accepted><OnlineDate><Year>2011</Year><Month>5</Month><Day>29</Day></OnlineDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>2011</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Cheryl</GivenName><GivenName>E.</GivenName><FamilyName>Myers</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Paul</GivenName><FamilyName>Hanavan</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Kwasi</GivenName><FamilyName>Antwi</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>Daruka</GivenName><FamilyName>Mahadevan</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>A.</GivenName><GivenName>Jamal</GivenName><FamilyName>Nadeem</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>Laurence</GivenName><FamilyName>Cooke</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff4"><AuthorName DisplayOrder="Western"><GivenName>Adrienne</GivenName><GivenName>C.</GivenName><FamilyName>Scheck</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Zachary</GivenName><FamilyName>Laughrey</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Douglas</GivenName><GivenName>F.</GivenName><FamilyName>Lake</FamilyName></AuthorName><Contact><Phone>+1-480-7279579</Phone><Fax>+1-480-9650098</Fax><Email>douglas.lake@asu.edu</Email></Contact></Author><Affiliation ID="Aff1"><OrgDivision>School of Life Sciences</OrgDivision><OrgName>Arizona State University</OrgName><OrgAddress><City>Tempe</City><State>AZ</State><Postcode>85287</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Department of Chemistry and Biochemistry</OrgDivision><OrgName>Arizona State University</OrgName><OrgAddress><City>Tempe</City><State>AZ</State><Postcode>85287</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgDivision>Department of Medicine, Arizona Cancer Center</OrgDivision><OrgName>University of Arizona</OrgName><OrgAddress><City>Tucson</City><State>AZ</State><Postcode>85724</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff4"><OrgName>Barrow Neurological Institute of SJHMC</OrgName><OrgAddress><City>Phoenix</City><State>AZ</State><Postcode>85013</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En" OutputMedium="All"><Heading>Abstract</Heading><Para>Genetic instability of tumor cells can result in translation of proteins that are out of frame, resulting in expression of neopeptides. These neopeptides are not self-proteins and therefore should be immunogenic. By eluting peptides from human glioblastoma multiforme (GBM) tumor cell surfaces and subjecting them to tandem mass spectrometry, we identified a novel peptide (KLWGLTPKVTPS) corresponding to a frameshift in the 3′ beta-hydroxysteroid dehydrogenase type 7 (HSD3B7) gene. HLA-binding algorithms predicted that a 9-amino acid sequence embedded in this peptide would bind to HLA-A*0201. We confirmed this prediction using an HLA-A*0201 refolding assay followed by live cell relative affinity assays, but also showed that the 12-mer binds to HLA-A*0201. Based on the 9-mer sequence, optimized peptide ligands (OPL) were designed and tested for their affinities to HLA-A*0201 and their abilities to elicit anti-peptide and CTL capable of killing GBM in vitro. Wild-type peptides as well as OPL induced anti-peptide CTL as measured by IFN-γ ELISPOTS. These CTL also killed GBM tumor cells in chromium-51 release assays. This study reports a new CTL target in GBM and further substantiates the concept that rational design and testing of multiple peptides for the same T-cell epitope elicits a broader response among different individuals than single peptide immunization.</Para></Abstract><KeywordGroup Language="En" OutputMedium="All"><Heading>Keywords</Heading><Keyword>Cytotoxic T lymphocytes</Keyword><Keyword>Optimized peptide ligand</Keyword><Keyword>Glioblastoma multiforme</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>CTL recognition of a novel HLA-A*0201-binding peptide derived from glioblastoma multiforme tumor cells</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>CTL recognition of a novel HLA-A*0201-binding peptide derived from glioblastoma multiforme tumor cells</title></titleInfo><name type="personal"><namePart type="given">Cheryl</namePart><namePart type="given">E.</namePart><namePart type="family">Myers</namePart><affiliation>School of Life Sciences, Arizona State University, 85287, Tempe, AZ, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Paul</namePart><namePart type="family">Hanavan</namePart><affiliation>School of Life Sciences, Arizona State University, 85287, Tempe, AZ, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Kwasi</namePart><namePart type="family">Antwi</namePart><affiliation>School of Life Sciences, Arizona State University, 85287, Tempe, AZ, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Daruka</namePart><namePart type="family">Mahadevan</namePart><affiliation>Department of Medicine, Arizona Cancer Center, University of Arizona, 85724, Tucson, AZ, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="given">Jamal</namePart><namePart type="family">Nadeem</namePart><affiliation>Department of Medicine, Arizona Cancer Center, University of Arizona, 85724, Tucson, AZ, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Laurence</namePart><namePart type="family">Cooke</namePart><affiliation>Department of Medicine, Arizona Cancer Center, University of Arizona, 85724, Tucson, AZ, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Adrienne</namePart><namePart type="given">C.</namePart><namePart type="family">Scheck</namePart><affiliation>Barrow Neurological Institute of SJHMC, 85013, Phoenix, AZ, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Zachary</namePart><namePart type="family">Laughrey</namePart><affiliation>Department of Chemistry and Biochemistry, Arizona State University, 85287, Tempe, AZ, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal" displayLabel="corresp"><namePart type="given">Douglas</namePart><namePart type="given">F.</namePart><namePart type="family">Lake</namePart><affiliation>School of Life Sciences, Arizona State University, 85287, Tempe, AZ, USA</affiliation><affiliation>E-mail: douglas.lake@asu.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</publisher><place><placeTerm type="text">Berlin/Heidelberg</placeTerm></place><dateCreated encoding="w3cdtf">2010-03-24</dateCreated><dateIssued encoding="w3cdtf">2011-09-01</dateIssued><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Genetic instability of tumor cells can result in translation of proteins that are out of frame, resulting in expression of neopeptides. These neopeptides are not self-proteins and therefore should be immunogenic. By eluting peptides from human glioblastoma multiforme (GBM) tumor cell surfaces and subjecting them to tandem mass spectrometry, we identified a novel peptide (KLWGLTPKVTPS) corresponding to a frameshift in the 3′ beta-hydroxysteroid dehydrogenase type 7 (HSD3B7) gene. HLA-binding algorithms predicted that a 9-amino acid sequence embedded in this peptide would bind to HLA-A*0201. We confirmed this prediction using an HLA-A*0201 refolding assay followed by live cell relative affinity assays, but also showed that the 12-mer binds to HLA-A*0201. Based on the 9-mer sequence, optimized peptide ligands (OPL) were designed and tested for their affinities to HLA-A*0201 and their abilities to elicit anti-peptide and CTL capable of killing GBM in vitro. Wild-type peptides as well as OPL induced anti-peptide CTL as measured by IFN-γ ELISPOTS. These CTL also killed GBM tumor cells in chromium-51 release assays. This study reports a new CTL target in GBM and further substantiates the concept that rational design and testing of multiple peptides for the same T-cell epitope elicits a broader response among different individuals than single peptide immunization.</abstract><note>Original article</note><subject lang="en"><genre>Keywords</genre><topic>Cytotoxic T lymphocytes</topic><topic>Optimized peptide ligand</topic><topic>Glioblastoma multiforme</topic></subject><relatedItem type="host"><titleInfo><title>Cancer Immunology, Immunotherapy</title></titleInfo><titleInfo type="abbreviated"><title>Cancer Immunol Immunother</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">2011-08-24</dateIssued><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><subject><genre>Medicine & Public Health</genre><topic>Oncology</topic><topic>Immunology</topic><topic>Cancer Research</topic></subject><identifier type="ISSN">0340-7004</identifier><identifier type="eISSN">1432-0851</identifier><identifier type="JournalID">262</identifier><identifier type="IssueArticleCount">14</identifier><identifier type="VolumeIssueCount">12</identifier><part><date>2011</date><detail type="volume"><number>60</number><caption>vol.</caption></detail><detail type="issue"><number>9</number><caption>no.</caption></detail><extent unit="pages"><start>1319</start><end>1332</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 2011</recordOrigin></recordInfo></relatedItem><identifier type="istex">30E50702B58C550D63EB656274326731E42B8D00</identifier><identifier type="ark">ark:/67375/VQC-DV51M98B-8</identifier><identifier type="DOI">10.1007/s00262-011-1032-4</identifier><identifier type="ArticleID">1032</identifier><identifier type="ArticleID">s00262-011-1032-4</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 2011</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, 2011</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-DV51M98B-8/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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