Characterization and Serologic Analysis of the Treponema pallidum Proteome
Treponema pallidum subsp. pallidum is the causative agent of syphilis, a sexually transmitted disease characterized by widespread tissue dissemination and chronic infection. In this study, we analyzed the proteome of T. pallidum by the isoelectric focusing (IEF) and nonequilibrating pH gel electroph...
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| Veröffentlicht in: | Infection and Immunity 2010-06, Vol.78 (6), p.2631-2643 |
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| creator | McGill, Melanie A Edmondson, Diane G Carroll, James A Cook, Richard G Orkiszewski, Ralph S Norris, Steven J |
| description | Treponema pallidum subsp. pallidum is the causative agent of syphilis, a sexually transmitted disease characterized by widespread tissue dissemination and chronic infection. In this study, we analyzed the proteome of T. pallidum by the isoelectric focusing (IEF) and nonequilibrating pH gel electrophoresis (NEPHGE) forms of two-dimensional gel electrophoresis (2DGE), coupled with matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis. We determined the identity of 148 T. pallidum protein spots, representing 88 T. pallidum polypeptides; 63 of these polypeptides had not been identified previously at the protein level. To examine which of these proteins are important in the antibody response to syphilis, we performed immunoblot analysis using infected rabbit sera or human sera from patients at different stages of syphilis infection. Twenty-nine previously described antigens (predominantly lipoproteins) were detected, as were a number of previously unidentified antigens. The reactivity patterns obtained with sera from infected rabbits and humans were similar; these patterns included a subset of antigens reactive with all serum samples tested, including CfpA, MglB-2, TmpA, TmpB, flagellins, and the 47-kDa, 17-kDa, and 15-kDa lipoproteins. A unique group of antigens specifically reactive with infected human serum was also identified and included the previously described antigen TpF1 and the hypothetical proteins TP0584, TP0608, and TP0965. This combined proteomic and serologic analysis further delineates the antigens potentially useful as vaccine candidates or diagnostic markers and may provide insight into the host-pathogen interactions that occur during T. pallidum infection. |
| doi_str_mv | 10.1128/IAI.00173-10 |
| format | Article |
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In this study, we analyzed the proteome of T. pallidum by the isoelectric focusing (IEF) and nonequilibrating pH gel electrophoresis (NEPHGE) forms of two-dimensional gel electrophoresis (2DGE), coupled with matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis. We determined the identity of 148 T. pallidum protein spots, representing 88 T. pallidum polypeptides; 63 of these polypeptides had not been identified previously at the protein level. To examine which of these proteins are important in the antibody response to syphilis, we performed immunoblot analysis using infected rabbit sera or human sera from patients at different stages of syphilis infection. Twenty-nine previously described antigens (predominantly lipoproteins) were detected, as were a number of previously unidentified antigens. The reactivity patterns obtained with sera from infected rabbits and humans were similar; these patterns included a subset of antigens reactive with all serum samples tested, including CfpA, MglB-2, TmpA, TmpB, flagellins, and the 47-kDa, 17-kDa, and 15-kDa lipoproteins. A unique group of antigens specifically reactive with infected human serum was also identified and included the previously described antigen TpF1 and the hypothetical proteins TP0584, TP0608, and TP0965. This combined proteomic and serologic analysis further delineates the antigens potentially useful as vaccine candidates or diagnostic markers and may provide insight into the host-pathogen interactions that occur during T. pallidum infection.</description><identifier>ISSN: 0019-9567</identifier><identifier>EISSN: 1098-5522</identifier><identifier>DOI: 10.1128/IAI.00173-10</identifier><identifier>PMID: 20385758</identifier><identifier>CODEN: INFIBR</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Antibodies, Bacterial - blood ; Antibody response ; Antigens, Bacterial - analysis ; Antigens, Bacterial - chemistry ; Antigens, Bacterial - immunology ; Bacterial Proteins - analysis ; Bacterial Proteins - chemistry ; Bacterial Proteins - immunology ; Bacteriology ; Biological and medical sciences ; Blotting, Western ; Chronic infection ; Combined vaccines ; Electrophoresis, Gel, Two-Dimensional ; Flagellin ; Flight ; Fundamental and applied biological sciences. Psychology ; Gel electrophoresis ; Globus pallidus ; Host-pathogen interactions ; Humans ; Isoelectric Focusing ; Lasers ; Lipoproteins ; Mice ; Mice, Inbred BALB C ; Microbiology ; Miscellaneous ; Molecular Pathogenesis ; Molecular Weight ; pH effects ; Proteins ; Proteome - analysis ; proteomics ; Rabbits ; Sexually-transmitted diseases ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Syphilis ; Syphilis - immunology ; Treponema pallidum ; Treponema pallidum - chemistry ; Treponema pallidum - immunology</subject><ispartof>Infection and Immunity, 2010-06, Vol.78 (6), p.2631-2643</ispartof><rights>2015 INIST-CNRS</rights><rights>Copyright © 2010, American Society for Microbiology 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c538t-8a700109ce308c8739d85d9caad8e8a76fb88f106dc3efb7718ba969763e52da3</citedby><cites>FETCH-LOGICAL-c538t-8a700109ce308c8739d85d9caad8e8a76fb88f106dc3efb7718ba969763e52da3</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/PMC2876534/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2876534/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,3175,3176,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22811877$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20385758$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McGill, Melanie A</creatorcontrib><creatorcontrib>Edmondson, Diane G</creatorcontrib><creatorcontrib>Carroll, James A</creatorcontrib><creatorcontrib>Cook, Richard G</creatorcontrib><creatorcontrib>Orkiszewski, Ralph S</creatorcontrib><creatorcontrib>Norris, Steven J</creatorcontrib><title>Characterization and Serologic Analysis of the Treponema pallidum Proteome</title><title>Infection and Immunity</title><addtitle>Infect Immun</addtitle><description>Treponema pallidum subsp. pallidum is the causative agent of syphilis, a sexually transmitted disease characterized by widespread tissue dissemination and chronic infection. In this study, we analyzed the proteome of T. pallidum by the isoelectric focusing (IEF) and nonequilibrating pH gel electrophoresis (NEPHGE) forms of two-dimensional gel electrophoresis (2DGE), coupled with matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis. We determined the identity of 148 T. pallidum protein spots, representing 88 T. pallidum polypeptides; 63 of these polypeptides had not been identified previously at the protein level. To examine which of these proteins are important in the antibody response to syphilis, we performed immunoblot analysis using infected rabbit sera or human sera from patients at different stages of syphilis infection. Twenty-nine previously described antigens (predominantly lipoproteins) were detected, as were a number of previously unidentified antigens. The reactivity patterns obtained with sera from infected rabbits and humans were similar; these patterns included a subset of antigens reactive with all serum samples tested, including CfpA, MglB-2, TmpA, TmpB, flagellins, and the 47-kDa, 17-kDa, and 15-kDa lipoproteins. A unique group of antigens specifically reactive with infected human serum was also identified and included the previously described antigen TpF1 and the hypothetical proteins TP0584, TP0608, and TP0965. This combined proteomic and serologic analysis further delineates the antigens potentially useful as vaccine candidates or diagnostic markers and may provide insight into the host-pathogen interactions that occur during T. pallidum infection.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antibodies, Bacterial - blood</subject><subject>Antibody response</subject><subject>Antigens, Bacterial - analysis</subject><subject>Antigens, Bacterial - chemistry</subject><subject>Antigens, Bacterial - immunology</subject><subject>Bacterial Proteins - analysis</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - immunology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Chronic infection</subject><subject>Combined vaccines</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Flagellin</subject><subject>Flight</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gel electrophoresis</subject><subject>Globus pallidus</subject><subject>Host-pathogen interactions</subject><subject>Humans</subject><subject>Isoelectric Focusing</subject><subject>Lasers</subject><subject>Lipoproteins</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Molecular Pathogenesis</subject><subject>Molecular Weight</subject><subject>pH effects</subject><subject>Proteins</subject><subject>Proteome - analysis</subject><subject>proteomics</subject><subject>Rabbits</subject><subject>Sexually-transmitted diseases</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Syphilis</subject><subject>Syphilis - immunology</subject><subject>Treponema pallidum</subject><subject>Treponema pallidum - chemistry</subject><subject>Treponema pallidum - immunology</subject><issn>0019-9567</issn><issn>1098-5522</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U1v1DAQBmALgehSuHGGcEBcSPFHEo8vSKsVH4sqgdT2bM06k41REm_tLKj8elx2KXDiZNnzaDz2y9hTwc-EkPBmvVyfcS60KgW_xxaCGyjrWsr7bJGPTWnqRp-wRyl9zduqquAhO5FcQa1rWLBPqx4jupmi_4GzD1OBU1tcUAxD2HpXLCccbpJPReiKuafiMtIuTDRiscNh8O1-LL7EMFMY6TF70OGQ6MlxPWVX799drj6W558_rFfL89LVCuYSUOdBuHGkODjQyrRQt8YhtkC52HQbgE7wpnWKuo3WAjZoGqMbRbVsUZ2yt4e-u_1mpNbRNEcc7C76EeONDejtv5XJ93YbvlkJuqlVlRu8OjaI4XpPabajT46GAScK-2R11XAN2pj_S6WEAC1klq8P0sWQUqTubh7B7W1ONudkf-WUTzJ_9vcb7vDvYDJ4eQSYHA5dxMn59MdJuL1YZ_fi4Hq_7b_7SBbTaH3-Aw22sbJRIpvnB9NhsLiNuc_VheRCcQFVpbL5CdOnr9g</recordid><startdate>20100601</startdate><enddate>20100601</enddate><creator>McGill, Melanie A</creator><creator>Edmondson, Diane G</creator><creator>Carroll, James A</creator><creator>Cook, Richard G</creator><creator>Orkiszewski, Ralph S</creator><creator>Norris, Steven J</creator><general>American Society for Microbiology</general><general>American Society for Microbiology (ASM)</general><scope>FBQ</scope><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>7X8</scope><scope>7QL</scope><scope>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>5PM</scope></search><sort><creationdate>20100601</creationdate><title>Characterization and Serologic Analysis of the Treponema pallidum Proteome</title><author>McGill, Melanie A ; Edmondson, Diane G ; Carroll, James A ; Cook, Richard G ; Orkiszewski, Ralph S ; Norris, Steven J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c538t-8a700109ce308c8739d85d9caad8e8a76fb88f106dc3efb7718ba969763e52da3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antibodies, Bacterial - blood</topic><topic>Antibody response</topic><topic>Antigens, Bacterial - analysis</topic><topic>Antigens, Bacterial - chemistry</topic><topic>Antigens, Bacterial - immunology</topic><topic>Bacterial Proteins - analysis</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - immunology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Chronic infection</topic><topic>Combined vaccines</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Flagellin</topic><topic>Flight</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gel electrophoresis</topic><topic>Globus pallidus</topic><topic>Host-pathogen interactions</topic><topic>Humans</topic><topic>Isoelectric Focusing</topic><topic>Lasers</topic><topic>Lipoproteins</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Molecular Pathogenesis</topic><topic>Molecular Weight</topic><topic>pH effects</topic><topic>Proteins</topic><topic>Proteome - analysis</topic><topic>proteomics</topic><topic>Rabbits</topic><topic>Sexually-transmitted diseases</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Syphilis</topic><topic>Syphilis - immunology</topic><topic>Treponema pallidum</topic><topic>Treponema pallidum - chemistry</topic><topic>Treponema pallidum - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McGill, Melanie A</creatorcontrib><creatorcontrib>Edmondson, Diane G</creatorcontrib><creatorcontrib>Carroll, James A</creatorcontrib><creatorcontrib>Cook, Richard G</creatorcontrib><creatorcontrib>Orkiszewski, Ralph S</creatorcontrib><creatorcontrib>Norris, Steven J</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Infection and Immunity</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McGill, Melanie A</au><au>Edmondson, Diane G</au><au>Carroll, James A</au><au>Cook, Richard G</au><au>Orkiszewski, Ralph S</au><au>Norris, Steven J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and Serologic Analysis of the Treponema pallidum Proteome</atitle><jtitle>Infection and Immunity</jtitle><addtitle>Infect Immun</addtitle><date>2010-06-01</date><risdate>2010</risdate><volume>78</volume><issue>6</issue><spage>2631</spage><epage>2643</epage><pages>2631-2643</pages><issn>0019-9567</issn><eissn>1098-5522</eissn><coden>INFIBR</coden><abstract>Treponema pallidum subsp. pallidum is the causative agent of syphilis, a sexually transmitted disease characterized by widespread tissue dissemination and chronic infection. In this study, we analyzed the proteome of T. pallidum by the isoelectric focusing (IEF) and nonequilibrating pH gel electrophoresis (NEPHGE) forms of two-dimensional gel electrophoresis (2DGE), coupled with matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis. We determined the identity of 148 T. pallidum protein spots, representing 88 T. pallidum polypeptides; 63 of these polypeptides had not been identified previously at the protein level. To examine which of these proteins are important in the antibody response to syphilis, we performed immunoblot analysis using infected rabbit sera or human sera from patients at different stages of syphilis infection. Twenty-nine previously described antigens (predominantly lipoproteins) were detected, as were a number of previously unidentified antigens. The reactivity patterns obtained with sera from infected rabbits and humans were similar; these patterns included a subset of antigens reactive with all serum samples tested, including CfpA, MglB-2, TmpA, TmpB, flagellins, and the 47-kDa, 17-kDa, and 15-kDa lipoproteins. A unique group of antigens specifically reactive with infected human serum was also identified and included the previously described antigen TpF1 and the hypothetical proteins TP0584, TP0608, and TP0965. This combined proteomic and serologic analysis further delineates the antigens potentially useful as vaccine candidates or diagnostic markers and may provide insight into the host-pathogen interactions that occur during T. pallidum infection.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>20385758</pmid><doi>10.1128/IAI.00173-10</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Analytical, structural and metabolic biochemistry Animals Antibodies, Bacterial - blood Antibody response Antigens, Bacterial - analysis Antigens, Bacterial - chemistry Antigens, Bacterial - immunology Bacterial Proteins - analysis Bacterial Proteins - chemistry Bacterial Proteins - immunology Bacteriology Biological and medical sciences Blotting, Western Chronic infection Combined vaccines Electrophoresis, Gel, Two-Dimensional Flagellin Flight Fundamental and applied biological sciences. Psychology Gel electrophoresis Globus pallidus Host-pathogen interactions Humans Isoelectric Focusing Lasers Lipoproteins Mice Mice, Inbred BALB C Microbiology Miscellaneous Molecular Pathogenesis Molecular Weight pH effects Proteins Proteome - analysis proteomics Rabbits Sexually-transmitted diseases Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Syphilis Syphilis - immunology Treponema pallidum Treponema pallidum - chemistry Treponema pallidum - immunology |
| title | Characterization and Serologic Analysis of the Treponema pallidum Proteome |
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