Identification of novel immunogenic Mycobacterium tuberculosis peptides that stimulate mononuclear cells from immune donors
Abstract Proteins which are secreted or associated with the cell envelope of Mycobacterium tuberculosis may contain protective T-cell epitopes. Prior to this study, a recombinant clone bank of enzymatically active M. tuberculosis-alkaline phosphatase fusions, were screened for immunogenicity in a mu...
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Veröffentlicht in: | FEMS microbiology letters 1999-08, Vol.177 (1), p.123-130 |
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creator | Moran, Alison J. Doran, James L. Wu, Jiong Treit, Janice D. Ekpo, Pattama Kerr, Valerie J. Roberts, Alan D. Orme, Ian M. Galant, Shirleen Ress, Stanley R. Nano, Francis E. |
description | Abstract
Proteins which are secreted or associated with the cell envelope of Mycobacterium tuberculosis may contain protective T-cell epitopes. Prior to this study, a recombinant clone bank of enzymatically active M. tuberculosis-alkaline phosphatase fusions, were screened for immunogenicity in a murine T-cell model. Five of these were selected for further study, and the IFN-γ secretion and proliferation of human PBMC from purified protein derivative-(PPD)-positive and PPD-negative donors were measured in response to oligopeptides, Mtb-PhoA fusions and one full-length protein. Epitopes from four of the five selected antigens were immunoreactive in the human model and corresponded to cytochrome d ubiquinol oxidase, cytochrome c oxidase subunit II, MTV005.02 and MTV033.08. Thus, this strategy identified novel human immunogenic peptides as possible candidates for a subunit vaccine. |
doi_str_mv | 10.1111/j.1574-6968.1999.tb13722.x |
format | Article |
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Proteins which are secreted or associated with the cell envelope of Mycobacterium tuberculosis may contain protective T-cell epitopes. Prior to this study, a recombinant clone bank of enzymatically active M. tuberculosis-alkaline phosphatase fusions, were screened for immunogenicity in a murine T-cell model. Five of these were selected for further study, and the IFN-γ secretion and proliferation of human PBMC from purified protein derivative-(PPD)-positive and PPD-negative donors were measured in response to oligopeptides, Mtb-PhoA fusions and one full-length protein. Epitopes from four of the five selected antigens were immunoreactive in the human model and corresponded to cytochrome d ubiquinol oxidase, cytochrome c oxidase subunit II, MTV005.02 and MTV033.08. Thus, this strategy identified novel human immunogenic peptides as possible candidates for a subunit vaccine.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1999.tb13722.x</identifier><identifier>PMID: 10436930</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Alkaline phosphatase ; Alkaline Phosphatase - chemistry ; Alkaline Phosphatase - immunology ; Amino Acid Sequence ; Antigens ; Antigens, Bacterial - chemistry ; Antigens, Bacterial - immunology ; Bacterial Proteins - chemistry ; Bacterial Proteins - immunology ; Bacteriology ; Biological and medical sciences ; Cloning, Molecular ; Cytochrome ; Cytochrome-c oxidase ; Cytochromes ; Electron Transport Complex IV - genetics ; Electron Transport Complex IV - metabolism ; Epitopes ; Epitopes - immunology ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; g-Interferon ; Humans ; Immunogenicity ; Interferon-gamma - biosynthesis ; Leukocytes (mononuclear) ; Lymphocyte Activation ; Lymphocytes - immunology ; Lymphocytes T ; Microbiology ; Molecular Sequence Data ; Mycobacterium tuberculosis ; Mycobacterium tuberculosis - immunology ; Oligopeptides ; Oxidase ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Peptides ; Peripheral blood mononuclear cells ; Proteins ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - immunology ; Tuberculin ; Tuberculosis ; Tuberculosis - immunology ; T‐cell epitope ; Ubiquinol ; Ubiquinol oxidase ; Vaccine candidate ; γ-Interferon</subject><ispartof>FEMS microbiology letters, 1999-08, Vol.177 (1), p.123-130</ispartof><rights>1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. 1999</rights><rights>1999 INIST-CNRS</rights><rights>1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4363-251f6e2f5c7b71024dc36e6f02c64fd42c4d8eb0d3b0e200ac9d5fa884f0d9833</citedby><cites>FETCH-LOGICAL-c4363-251f6e2f5c7b71024dc36e6f02c64fd42c4d8eb0d3b0e200ac9d5fa884f0d9833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.1999.tb13722.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.1999.tb13722.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1893127$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10436930$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moran, Alison J.</creatorcontrib><creatorcontrib>Doran, James L.</creatorcontrib><creatorcontrib>Wu, Jiong</creatorcontrib><creatorcontrib>Treit, Janice D.</creatorcontrib><creatorcontrib>Ekpo, Pattama</creatorcontrib><creatorcontrib>Kerr, Valerie J.</creatorcontrib><creatorcontrib>Roberts, Alan D.</creatorcontrib><creatorcontrib>Orme, Ian M.</creatorcontrib><creatorcontrib>Galant, Shirleen</creatorcontrib><creatorcontrib>Ress, Stanley R.</creatorcontrib><creatorcontrib>Nano, Francis E.</creatorcontrib><title>Identification of novel immunogenic Mycobacterium tuberculosis peptides that stimulate mononuclear cells from immune donors</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
Proteins which are secreted or associated with the cell envelope of Mycobacterium tuberculosis may contain protective T-cell epitopes. Prior to this study, a recombinant clone bank of enzymatically active M. tuberculosis-alkaline phosphatase fusions, were screened for immunogenicity in a murine T-cell model. Five of these were selected for further study, and the IFN-γ secretion and proliferation of human PBMC from purified protein derivative-(PPD)-positive and PPD-negative donors were measured in response to oligopeptides, Mtb-PhoA fusions and one full-length protein. Epitopes from four of the five selected antigens were immunoreactive in the human model and corresponded to cytochrome d ubiquinol oxidase, cytochrome c oxidase subunit II, MTV005.02 and MTV033.08. Thus, this strategy identified novel human immunogenic peptides as possible candidates for a subunit vaccine.</description><subject>Alkaline phosphatase</subject><subject>Alkaline Phosphatase - chemistry</subject><subject>Alkaline Phosphatase - immunology</subject><subject>Amino Acid Sequence</subject><subject>Antigens</subject><subject>Antigens, Bacterial - chemistry</subject><subject>Antigens, Bacterial - immunology</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - immunology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>Cytochrome</subject><subject>Cytochrome-c oxidase</subject><subject>Cytochromes</subject><subject>Electron Transport Complex IV - genetics</subject><subject>Electron Transport Complex IV - metabolism</subject><subject>Epitopes</subject><subject>Epitopes - immunology</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>g-Interferon</subject><subject>Humans</subject><subject>Immunogenicity</subject><subject>Interferon-gamma - biosynthesis</subject><subject>Leukocytes (mononuclear)</subject><subject>Lymphocyte Activation</subject><subject>Lymphocytes - immunology</subject><subject>Lymphocytes T</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - immunology</subject><subject>Oligopeptides</subject><subject>Oxidase</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Peptides</subject><subject>Peripheral blood mononuclear cells</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - immunology</subject><subject>Tuberculin</subject><subject>Tuberculosis</subject><subject>Tuberculosis - immunology</subject><subject>T‐cell epitope</subject><subject>Ubiquinol</subject><subject>Ubiquinol oxidase</subject><subject>Vaccine candidate</subject><subject>γ-Interferon</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqVkUuLFDEUhYMoTjv6FySouKsyj3rFxYAMjg704EbXIZXcaJqqSpmHTuOft4pqVEQRs7mL-52TezgIPaGkpMt7cShp3VZFI5qupEKIMvWUt4yVt3fQ7sfqLtoR3nYFJaI9Qw9iPBBCKkaa--iMkoo3gpMd-nZtYErOOq2S8xP2Fk_-CwzYjWOe_EeYnMY3R-17pRMEl0eccg9B58FHF_EMc3IGIk6fVMIxuTEPKgEe_eSnrAdQAWsYhoht8OPmCtgs2xAfontWDREeneY5-nD1-v3l22L_7s315at9oZcrecFqahtgttZt31LCKqN5A40lTDeVNRXTlemgJ4b3BBghSgtTW9V1lSVGdJyfo-eb7xz85wwxydHF9Sg1gc9RNkLUhNJ_g7TjjDYdXcCnv4EHn8O0hJCMU9rWdVWvdi83SgcfYwAr5-BGFY6SErk2KQ9yrUuudcm1SXlqUt4u4senL3I_gvlFulW3AM9OgIpaDTaoSbv4k-sEp6xdsIsN--oGOP7HBfLqZk_ZmqLeDHye_yIv_hTgO7b6zZU</recordid><startdate>199908</startdate><enddate>199908</enddate><creator>Moran, Alison J.</creator><creator>Doran, James L.</creator><creator>Wu, Jiong</creator><creator>Treit, Janice D.</creator><creator>Ekpo, Pattama</creator><creator>Kerr, Valerie J.</creator><creator>Roberts, Alan D.</creator><creator>Orme, Ian M.</creator><creator>Galant, Shirleen</creator><creator>Ress, Stanley R.</creator><creator>Nano, Francis E.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</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>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</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>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>199908</creationdate><title>Identification of novel immunogenic Mycobacterium tuberculosis peptides that stimulate mononuclear cells from immune donors</title><author>Moran, Alison J. ; Doran, James L. ; Wu, Jiong ; Treit, Janice D. ; Ekpo, Pattama ; Kerr, Valerie J. ; Roberts, Alan D. ; Orme, Ian M. ; Galant, Shirleen ; Ress, Stanley R. ; Nano, Francis E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4363-251f6e2f5c7b71024dc36e6f02c64fd42c4d8eb0d3b0e200ac9d5fa884f0d9833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Alkaline phosphatase</topic><topic>Alkaline Phosphatase - chemistry</topic><topic>Alkaline Phosphatase - immunology</topic><topic>Amino Acid Sequence</topic><topic>Antigens</topic><topic>Antigens, Bacterial - chemistry</topic><topic>Antigens, Bacterial - immunology</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - immunology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>Cytochrome</topic><topic>Cytochrome-c oxidase</topic><topic>Cytochromes</topic><topic>Electron Transport Complex IV - genetics</topic><topic>Electron Transport Complex IV - metabolism</topic><topic>Epitopes</topic><topic>Epitopes - immunology</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>g-Interferon</topic><topic>Humans</topic><topic>Immunogenicity</topic><topic>Interferon-gamma - biosynthesis</topic><topic>Leukocytes (mononuclear)</topic><topic>Lymphocyte Activation</topic><topic>Lymphocytes - immunology</topic><topic>Lymphocytes T</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Mycobacterium tuberculosis</topic><topic>Mycobacterium tuberculosis - immunology</topic><topic>Oligopeptides</topic><topic>Oxidase</topic><topic>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</topic><topic>Peptides</topic><topic>Peripheral blood mononuclear cells</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - immunology</topic><topic>Tuberculin</topic><topic>Tuberculosis</topic><topic>Tuberculosis - immunology</topic><topic>T‐cell epitope</topic><topic>Ubiquinol</topic><topic>Ubiquinol oxidase</topic><topic>Vaccine candidate</topic><topic>γ-Interferon</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moran, Alison J.</creatorcontrib><creatorcontrib>Doran, James L.</creatorcontrib><creatorcontrib>Wu, Jiong</creatorcontrib><creatorcontrib>Treit, Janice D.</creatorcontrib><creatorcontrib>Ekpo, Pattama</creatorcontrib><creatorcontrib>Kerr, Valerie J.</creatorcontrib><creatorcontrib>Roberts, Alan D.</creatorcontrib><creatorcontrib>Orme, Ian M.</creatorcontrib><creatorcontrib>Galant, Shirleen</creatorcontrib><creatorcontrib>Ress, Stanley R.</creatorcontrib><creatorcontrib>Nano, Francis E.</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS 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>Public Health Database</collection><collection>Technology Research 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 One Sustainability</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>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - 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Proteins which are secreted or associated with the cell envelope of Mycobacterium tuberculosis may contain protective T-cell epitopes. Prior to this study, a recombinant clone bank of enzymatically active M. tuberculosis-alkaline phosphatase fusions, were screened for immunogenicity in a murine T-cell model. Five of these were selected for further study, and the IFN-γ secretion and proliferation of human PBMC from purified protein derivative-(PPD)-positive and PPD-negative donors were measured in response to oligopeptides, Mtb-PhoA fusions and one full-length protein. Epitopes from four of the five selected antigens were immunoreactive in the human model and corresponded to cytochrome d ubiquinol oxidase, cytochrome c oxidase subunit II, MTV005.02 and MTV033.08. Thus, this strategy identified novel human immunogenic peptides as possible candidates for a subunit vaccine.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>10436930</pmid><doi>10.1111/j.1574-6968.1999.tb13722.x</doi><tpages>8</tpages></addata></record> |
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source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
subjects | Alkaline phosphatase Alkaline Phosphatase - chemistry Alkaline Phosphatase - immunology Amino Acid Sequence Antigens Antigens, Bacterial - chemistry Antigens, Bacterial - immunology Bacterial Proteins - chemistry Bacterial Proteins - immunology Bacteriology Biological and medical sciences Cloning, Molecular Cytochrome Cytochrome-c oxidase Cytochromes Electron Transport Complex IV - genetics Electron Transport Complex IV - metabolism Epitopes Epitopes - immunology Escherichia coli Fundamental and applied biological sciences. Psychology g-Interferon Humans Immunogenicity Interferon-gamma - biosynthesis Leukocytes (mononuclear) Lymphocyte Activation Lymphocytes - immunology Lymphocytes T Microbiology Molecular Sequence Data Mycobacterium tuberculosis Mycobacterium tuberculosis - immunology Oligopeptides Oxidase Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Peptides Peripheral blood mononuclear cells Proteins Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - immunology Tuberculin Tuberculosis Tuberculosis - immunology T‐cell epitope Ubiquinol Ubiquinol oxidase Vaccine candidate γ-Interferon |
title | Identification of novel immunogenic Mycobacterium tuberculosis peptides that stimulate mononuclear cells from immune donors |
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