A MAGE-1 antigenic peptide recognized by human cytolytic T lymphocytes on HLA-A2 tumor cells
"Cancer-germline" genes such as those of the MAGE family are expressed in many tumors and in male germline cells, but are silent in normal tissues. They encode shared tumor-specific antigens that have been used in therapeutic vaccination trials of cancer patients. It was previously demonst...
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| Veröffentlicht in: | Cancer Immunology, Immunotherapy Immunotherapy, 2005-12, Vol.54 (12), p.1214-1220 |
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| container_title | Cancer Immunology, Immunotherapy |
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| creator | OTTAVIANI, Sabrina YI ZHANG BOON, Thierry VAN DER BRUGGEN, Pierre |
| description | "Cancer-germline" genes such as those of the MAGE family are expressed in many tumors and in male germline cells, but are silent in normal tissues. They encode shared tumor-specific antigens that have been used in therapeutic vaccination trials of cancer patients. It was previously demonstrated that MAGE-1 peptide KVLEYVIKV was presented by HLA-A 0201 molecules on the surface of a human breast carcinoma cell line, but no human specific CTL had been isolated so far. Here, we have used HLA-A2/MAGE-1 fluorescent multimers to isolate from blood cells three human CTL clones that recognized the MAGE-1 peptide. These clones killed efficiently HLA-A2 tumor cells expressing MAGE-1, whether or not they were treated with IFN-gamma, suggesting that the MAGE-1 antigen is processed efficiently by both the standard proteasome and the immunoproteasome. These results indicate that the MAGE-1.A2 peptide can be used for antitumoral vaccination. |
| doi_str_mv | 10.1007/s00262-005-0705-2 |
| format | Article |
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They encode shared tumor-specific antigens that have been used in therapeutic vaccination trials of cancer patients. It was previously demonstrated that MAGE-1 peptide KVLEYVIKV was presented by HLA-A 0201 molecules on the surface of a human breast carcinoma cell line, but no human specific CTL had been isolated so far. Here, we have used HLA-A2/MAGE-1 fluorescent multimers to isolate from blood cells three human CTL clones that recognized the MAGE-1 peptide. These clones killed efficiently HLA-A2 tumor cells expressing MAGE-1, whether or not they were treated with IFN-gamma, suggesting that the MAGE-1 antigen is processed efficiently by both the standard proteasome and the immunoproteasome. These results indicate that the MAGE-1.A2 peptide can be used for antitumoral vaccination.</description><identifier>ISSN: 0340-7004</identifier><identifier>EISSN: 1432-0851</identifier><identifier>EISSN: 1365-2567</identifier><identifier>DOI: 10.1007/s00262-005-0705-2</identifier><identifier>PMID: 16025263</identifier><identifier>CODEN: CIIMDN</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Amino Acid Sequence ; Antigen Presentation ; Antigens ; Antigens, Neoplasm - immunology ; Antineoplastic agents ; Biological and medical sciences ; Breast cancer ; Cloning ; Genes ; HLA-A2 Antigen - analysis ; HLA-A2 Antigen - metabolism ; Humans ; Immunization ; Immunotherapy ; Lymphocytes ; Medical sciences ; Molecular Sequence Data ; Neoplasm Proteins - immunology ; Neoplasms - immunology ; Original ; Peptide Fragments - immunology ; Peptides ; Pharmacology. Drug treatments ; Proteasome Endopeptidase Complex - metabolism ; T-Lymphocytes, Cytotoxic - immunology ; Thymus gland ; Transgenic animals ; Tumors ; Vaccines</subject><ispartof>Cancer Immunology, Immunotherapy, 2005-12, Vol.54 (12), p.1214-1220</ispartof><rights>2005 INIST-CNRS</rights><rights>Springer-Verlag 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c443t-df7a7d9aad9b0926ffa0f929aa4f87d084c25bd2d2a077714e4546f72d77676b3</citedby><cites>FETCH-LOGICAL-c443t-df7a7d9aad9b0926ffa0f929aa4f87d084c25bd2d2a077714e4546f72d77676b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11032837/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11032837/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53770,53772</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17178404$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16025263$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>OTTAVIANI, Sabrina</creatorcontrib><creatorcontrib>YI ZHANG</creatorcontrib><creatorcontrib>BOON, Thierry</creatorcontrib><creatorcontrib>VAN DER BRUGGEN, Pierre</creatorcontrib><title>A MAGE-1 antigenic peptide recognized by human cytolytic T lymphocytes on HLA-A2 tumor cells</title><title>Cancer Immunology, Immunotherapy</title><addtitle>Cancer Immunol Immunother</addtitle><description>"Cancer-germline" genes such as those of the MAGE family are expressed in many tumors and in male germline cells, but are silent in normal tissues. They encode shared tumor-specific antigens that have been used in therapeutic vaccination trials of cancer patients. It was previously demonstrated that MAGE-1 peptide KVLEYVIKV was presented by HLA-A 0201 molecules on the surface of a human breast carcinoma cell line, but no human specific CTL had been isolated so far. Here, we have used HLA-A2/MAGE-1 fluorescent multimers to isolate from blood cells three human CTL clones that recognized the MAGE-1 peptide. These clones killed efficiently HLA-A2 tumor cells expressing MAGE-1, whether or not they were treated with IFN-gamma, suggesting that the MAGE-1 antigen is processed efficiently by both the standard proteasome and the immunoproteasome. These results indicate that the MAGE-1.A2 peptide can be used for antitumoral vaccination.</description><subject>Amino Acid Sequence</subject><subject>Antigen Presentation</subject><subject>Antigens</subject><subject>Antigens, Neoplasm - immunology</subject><subject>Antineoplastic agents</subject><subject>Biological and medical sciences</subject><subject>Breast cancer</subject><subject>Cloning</subject><subject>Genes</subject><subject>HLA-A2 Antigen - analysis</subject><subject>HLA-A2 Antigen - metabolism</subject><subject>Humans</subject><subject>Immunization</subject><subject>Immunotherapy</subject><subject>Lymphocytes</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Neoplasm Proteins - immunology</subject><subject>Neoplasms - immunology</subject><subject>Original</subject><subject>Peptide Fragments - immunology</subject><subject>Peptides</subject><subject>Pharmacology. Drug treatments</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>T-Lymphocytes, Cytotoxic - immunology</subject><subject>Thymus gland</subject><subject>Transgenic animals</subject><subject>Tumors</subject><subject>Vaccines</subject><issn>0340-7004</issn><issn>1432-0851</issn><issn>1365-2567</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkUFv1DAQhS0EokvhB3BBFhLcQseOY8cnFFWlRVrUS7khWY7t7KZK7GAnSOmvr1e7osCFi8d68_lpxg-htwQ-EQBxkQAopwVAVYDIB32GNoSVWakr8hxtoGRQCAB2hl6ldJ8vFKR8ic4IB1pRXm7QjwZ_a66vCoK1n_ud873Bk5vm3jocnQk73z84i9sV75dRe2zWOQzrnKk7PKzjtA9ZcQkHj2-2TdFQPC9jiNi4YUiv0YtOD8m9OdVz9P3L1d3lTbG9vf562WwLw1g5F7YTWliptZUtSMq7TkMnaRZYVwsLNTO0ai21VIMQgjDHKsY7Qa0QXPC2PEefj77T0o7OGufnqAc1xX7UcVVB9-rvju_3ahd-KUKgpHUpssPHk0MMPxeXZjX26bCD9i4sSfGac8kF_S9IBMiKVVUG3_8D3ocl-vwNipKSSUGIzBA5QiaGlKLrfs9MQB0iVseIVY5YHSJWhwne_bns04tTphn4cAJ0MnroovamT0-cIKJmwMpHkaetmA</recordid><startdate>20051201</startdate><enddate>20051201</enddate><creator>OTTAVIANI, Sabrina</creator><creator>YI ZHANG</creator><creator>BOON, Thierry</creator><creator>VAN DER BRUGGEN, Pierre</creator><general>Springer</general><general>Springer Nature B.V</general><general>Springer-Verlag</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>3V.</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20051201</creationdate><title>A MAGE-1 antigenic peptide recognized by human cytolytic T lymphocytes on HLA-A2 tumor cells</title><author>OTTAVIANI, Sabrina ; YI ZHANG ; BOON, Thierry ; VAN DER BRUGGEN, Pierre</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-df7a7d9aad9b0926ffa0f929aa4f87d084c25bd2d2a077714e4546f72d77676b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Antigen Presentation</topic><topic>Antigens</topic><topic>Antigens, Neoplasm - immunology</topic><topic>Antineoplastic agents</topic><topic>Biological and medical sciences</topic><topic>Breast cancer</topic><topic>Cloning</topic><topic>Genes</topic><topic>HLA-A2 Antigen - analysis</topic><topic>HLA-A2 Antigen - metabolism</topic><topic>Humans</topic><topic>Immunization</topic><topic>Immunotherapy</topic><topic>Lymphocytes</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Neoplasm Proteins - immunology</topic><topic>Neoplasms - immunology</topic><topic>Original</topic><topic>Peptide Fragments - immunology</topic><topic>Peptides</topic><topic>Pharmacology. Drug treatments</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>T-Lymphocytes, Cytotoxic - immunology</topic><topic>Thymus gland</topic><topic>Transgenic animals</topic><topic>Tumors</topic><topic>Vaccines</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>OTTAVIANI, Sabrina</creatorcontrib><creatorcontrib>YI ZHANG</creatorcontrib><creatorcontrib>BOON, Thierry</creatorcontrib><creatorcontrib>VAN DER BRUGGEN, Pierre</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>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cancer Immunology, Immunotherapy</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>OTTAVIANI, Sabrina</au><au>YI ZHANG</au><au>BOON, Thierry</au><au>VAN DER BRUGGEN, Pierre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A MAGE-1 antigenic peptide recognized by human cytolytic T lymphocytes on HLA-A2 tumor cells</atitle><jtitle>Cancer Immunology, Immunotherapy</jtitle><addtitle>Cancer Immunol Immunother</addtitle><date>2005-12-01</date><risdate>2005</risdate><volume>54</volume><issue>12</issue><spage>1214</spage><epage>1220</epage><pages>1214-1220</pages><issn>0340-7004</issn><eissn>1432-0851</eissn><eissn>1365-2567</eissn><coden>CIIMDN</coden><abstract>"Cancer-germline" genes such as those of the MAGE family are expressed in many tumors and in male germline cells, but are silent in normal tissues. They encode shared tumor-specific antigens that have been used in therapeutic vaccination trials of cancer patients. It was previously demonstrated that MAGE-1 peptide KVLEYVIKV was presented by HLA-A 0201 molecules on the surface of a human breast carcinoma cell line, but no human specific CTL had been isolated so far. Here, we have used HLA-A2/MAGE-1 fluorescent multimers to isolate from blood cells three human CTL clones that recognized the MAGE-1 peptide. These clones killed efficiently HLA-A2 tumor cells expressing MAGE-1, whether or not they were treated with IFN-gamma, suggesting that the MAGE-1 antigen is processed efficiently by both the standard proteasome and the immunoproteasome. These results indicate that the MAGE-1.A2 peptide can be used for antitumoral vaccination.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>16025263</pmid><doi>10.1007/s00262-005-0705-2</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Antigen Presentation Antigens Antigens, Neoplasm - immunology Antineoplastic agents Biological and medical sciences Breast cancer Cloning Genes HLA-A2 Antigen - analysis HLA-A2 Antigen - metabolism Humans Immunization Immunotherapy Lymphocytes Medical sciences Molecular Sequence Data Neoplasm Proteins - immunology Neoplasms - immunology Original Peptide Fragments - immunology Peptides Pharmacology. Drug treatments Proteasome Endopeptidase Complex - metabolism T-Lymphocytes, Cytotoxic - immunology Thymus gland Transgenic animals Tumors Vaccines |
| title | A MAGE-1 antigenic peptide recognized by human cytolytic T lymphocytes on HLA-A2 tumor cells |
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