Properties of repeat domain found in a novel protective antigen, SpaA, of Erysipelothrix rhusiopathiae
Erysipelothrix rhusiopathiae is a small gram-positive rod bacterium that causes erysipelas in swine and a variety of diseases in other animals and humans. Although live-attenuated or bacterin vaccines are effective in protecting against erysipelas, the genetic construction of their active antigen ha...
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| Veröffentlicht in: | Microbial pathogenesis 1998-08, Vol.25 (2), p.101-109 |
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| container_title | Microbial pathogenesis |
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| creator | MAKINO, S.-I YAMAMOTO, K MURAKAMI, S SHIRAHATA, T UEMURA, K SAWADA, T WAKAMOTO, H MORITA, Y |
| description | Erysipelothrix rhusiopathiae is a small gram-positive rod bacterium that causes erysipelas in swine and a variety of diseases in other animals and humans. Although live-attenuated or bacterin vaccines are effective in protecting against erysipelas, the genetic construction of their active antigen has not been identified. To clarify the surface antigen(s) involved in protective and arthritic response, using monoclonal antibody I2A against the surface proteins of E. rhusiopathiae, we identified a protective antigen, which consists of 606 amino acids. Analysis of deletion derivatives of the gene, spaA(surface protective antigen), showed that the SpaA protein binds tightly to the bacterial cell surface via eight repeat units with a GW-module consisting of 20 amino acids at the C-terminus. Although DeltaSpaA lacking their repeat units lost its ability to induce protection against E. rhusiopathiae infection, intact SpaA protein showed the protection. We conclude that the presence of repeat units is essential both for the binding of SpaA to the bacterial cell surface and for protection. We believe that the repeat region at the C-terminus should be a candidate for a subunit vaccine against erysipelas. |
| doi_str_mv | 10.1006/mpat.1998.0216 |
| format | Article |
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Although live-attenuated or bacterin vaccines are effective in protecting against erysipelas, the genetic construction of their active antigen has not been identified. To clarify the surface antigen(s) involved in protective and arthritic response, using monoclonal antibody I2A against the surface proteins of E. rhusiopathiae, we identified a protective antigen, which consists of 606 amino acids. Analysis of deletion derivatives of the gene, spaA(surface protective antigen), showed that the SpaA protein binds tightly to the bacterial cell surface via eight repeat units with a GW-module consisting of 20 amino acids at the C-terminus. Although DeltaSpaA lacking their repeat units lost its ability to induce protection against E. rhusiopathiae infection, intact SpaA protein showed the protection. We conclude that the presence of repeat units is essential both for the binding of SpaA to the bacterial cell surface and for protection. We believe that the repeat region at the C-terminus should be a candidate for a subunit vaccine against erysipelas.</description><identifier>ISSN: 0882-4010</identifier><identifier>EISSN: 1096-1208</identifier><identifier>DOI: 10.1006/mpat.1998.0216</identifier><identifier>PMID: 9712689</identifier><identifier>CODEN: MIPAEV</identifier><language>eng</language><publisher>Oxford: Elsevier</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Antigens, Bacterial - chemistry ; Antigens, Bacterial - genetics ; Antigens, Bacterial - immunology ; Antigens, Surface - chemistry ; Antigens, Surface - genetics ; Antigens, Surface - immunology ; Bacterial Proteins ; Bacteriology ; Biological and medical sciences ; Erysipelothrix - classification ; Erysipelothrix - genetics ; Erysipelothrix - immunology ; Erysipelothrix rhusiopathiae ; Escherichia coli - immunology ; Escherichia coli - physiology ; Fundamental and applied biological sciences. Psychology ; Genes, Bacterial ; Humans ; Mice ; Microbiology ; Molecular Sequence Data ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Sequence Alignment ; Sequence Deletion ; Sequence Homology, Amino Acid ; Serotyping ; Swine ; Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies</subject><ispartof>Microbial pathogenesis, 1998-08, Vol.25 (2), p.101-109</ispartof><rights>1998 INIST-CNRS</rights><rights>Copyright 1998 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2402711$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9712689$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MAKINO, S.-I</creatorcontrib><creatorcontrib>YAMAMOTO, K</creatorcontrib><creatorcontrib>MURAKAMI, S</creatorcontrib><creatorcontrib>SHIRAHATA, T</creatorcontrib><creatorcontrib>UEMURA, K</creatorcontrib><creatorcontrib>SAWADA, T</creatorcontrib><creatorcontrib>WAKAMOTO, H</creatorcontrib><creatorcontrib>MORITA, Y</creatorcontrib><title>Properties of repeat domain found in a novel protective antigen, SpaA, of Erysipelothrix rhusiopathiae</title><title>Microbial pathogenesis</title><addtitle>Microb Pathog</addtitle><description>Erysipelothrix rhusiopathiae is a small gram-positive rod bacterium that causes erysipelas in swine and a variety of diseases in other animals and humans. Although live-attenuated or bacterin vaccines are effective in protecting against erysipelas, the genetic construction of their active antigen has not been identified. To clarify the surface antigen(s) involved in protective and arthritic response, using monoclonal antibody I2A against the surface proteins of E. rhusiopathiae, we identified a protective antigen, which consists of 606 amino acids. Analysis of deletion derivatives of the gene, spaA(surface protective antigen), showed that the SpaA protein binds tightly to the bacterial cell surface via eight repeat units with a GW-module consisting of 20 amino acids at the C-terminus. Although DeltaSpaA lacking their repeat units lost its ability to induce protection against E. rhusiopathiae infection, intact SpaA protein showed the protection. We conclude that the presence of repeat units is essential both for the binding of SpaA to the bacterial cell surface and for protection. We believe that the repeat region at the C-terminus should be a candidate for a subunit vaccine against erysipelas.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Antigens, Bacterial - chemistry</subject><subject>Antigens, Bacterial - genetics</subject><subject>Antigens, Bacterial - immunology</subject><subject>Antigens, Surface - chemistry</subject><subject>Antigens, Surface - genetics</subject><subject>Antigens, Surface - immunology</subject><subject>Bacterial Proteins</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Erysipelothrix - classification</subject><subject>Erysipelothrix - genetics</subject><subject>Erysipelothrix - immunology</subject><subject>Erysipelothrix rhusiopathiae</subject><subject>Escherichia coli - immunology</subject><subject>Escherichia coli - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Bacterial</subject><subject>Humans</subject><subject>Mice</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Sequence Alignment</subject><subject>Sequence Deletion</subject><subject>Sequence Homology, Amino Acid</subject><subject>Serotyping</subject><subject>Swine</subject><subject>Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies</subject><issn>0882-4010</issn><issn>1096-1208</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1LAzEQxYMotVav3oQcxFO3TnbTbHIspX5AQUE9L2l21kZ2N2uSLfa_d8Xi1dMMvN8M7z1CLhnMGIC4bTodZ0wpOYOUiSMyZqBEwlKQx2QMUqYJBwan5CyEDwBQPFMjMlI5S4VUY1I9e9ehjxYDdRX12KGOtHSNti2tXN-WdFg0bd0Oa9p5F9FEu0Oq22jfsZ3Sl04vpj-3K78PtsPaxa23X9Rv-2Dd4G5rNZ6Tk0rXAS8Oc0Le7lavy4dk_XT_uFysk44pGZMUDIBMSyaM4CarNqycg6mGFMB1xrONkPm8LMscJdOc67mRKDeZFKJCngPPJuTm9-_g9LPHEIvGBoN1rVt0fSjygR0qmP8LspzxTCg1gFcHsN80WBadt432--LQ4KBfH3QdjK4rr1tjwx-WckhzxrJv5sGAGQ</recordid><startdate>19980801</startdate><enddate>19980801</enddate><creator>MAKINO, S.-I</creator><creator>YAMAMOTO, K</creator><creator>MURAKAMI, S</creator><creator>SHIRAHATA, T</creator><creator>UEMURA, K</creator><creator>SAWADA, T</creator><creator>WAKAMOTO, H</creator><creator>MORITA, Y</creator><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19980801</creationdate><title>Properties of repeat domain found in a novel protective antigen, SpaA, of Erysipelothrix rhusiopathiae</title><author>MAKINO, S.-I ; YAMAMOTO, K ; MURAKAMI, S ; SHIRAHATA, T ; UEMURA, K ; SAWADA, T ; WAKAMOTO, H ; MORITA, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p198t-20c0082d16c64c3fb1d50cf88204a343b6875ddd7e81a44a5c8e8b3866fe47043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Antigens, Bacterial - chemistry</topic><topic>Antigens, Bacterial - genetics</topic><topic>Antigens, Bacterial - immunology</topic><topic>Antigens, Surface - chemistry</topic><topic>Antigens, Surface - genetics</topic><topic>Antigens, Surface - immunology</topic><topic>Bacterial Proteins</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Erysipelothrix - classification</topic><topic>Erysipelothrix - genetics</topic><topic>Erysipelothrix - immunology</topic><topic>Erysipelothrix rhusiopathiae</topic><topic>Escherichia coli - immunology</topic><topic>Escherichia coli - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Bacterial</topic><topic>Humans</topic><topic>Mice</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Sequence Alignment</topic><topic>Sequence Deletion</topic><topic>Sequence Homology, Amino Acid</topic><topic>Serotyping</topic><topic>Swine</topic><topic>Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MAKINO, S.-I</creatorcontrib><creatorcontrib>YAMAMOTO, K</creatorcontrib><creatorcontrib>MURAKAMI, S</creatorcontrib><creatorcontrib>SHIRAHATA, T</creatorcontrib><creatorcontrib>UEMURA, K</creatorcontrib><creatorcontrib>SAWADA, T</creatorcontrib><creatorcontrib>WAKAMOTO, H</creatorcontrib><creatorcontrib>MORITA, Y</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Microbial pathogenesis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MAKINO, S.-I</au><au>YAMAMOTO, K</au><au>MURAKAMI, S</au><au>SHIRAHATA, T</au><au>UEMURA, K</au><au>SAWADA, T</au><au>WAKAMOTO, H</au><au>MORITA, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Properties of repeat domain found in a novel protective antigen, SpaA, of Erysipelothrix rhusiopathiae</atitle><jtitle>Microbial pathogenesis</jtitle><addtitle>Microb Pathog</addtitle><date>1998-08-01</date><risdate>1998</risdate><volume>25</volume><issue>2</issue><spage>101</spage><epage>109</epage><pages>101-109</pages><issn>0882-4010</issn><eissn>1096-1208</eissn><coden>MIPAEV</coden><abstract>Erysipelothrix rhusiopathiae is a small gram-positive rod bacterium that causes erysipelas in swine and a variety of diseases in other animals and humans. Although live-attenuated or bacterin vaccines are effective in protecting against erysipelas, the genetic construction of their active antigen has not been identified. To clarify the surface antigen(s) involved in protective and arthritic response, using monoclonal antibody I2A against the surface proteins of E. rhusiopathiae, we identified a protective antigen, which consists of 606 amino acids. Analysis of deletion derivatives of the gene, spaA(surface protective antigen), showed that the SpaA protein binds tightly to the bacterial cell surface via eight repeat units with a GW-module consisting of 20 amino acids at the C-terminus. Although DeltaSpaA lacking their repeat units lost its ability to induce protection against E. rhusiopathiae infection, intact SpaA protein showed the protection. We conclude that the presence of repeat units is essential both for the binding of SpaA to the bacterial cell surface and for protection. We believe that the repeat region at the C-terminus should be a candidate for a subunit vaccine against erysipelas.</abstract><cop>Oxford</cop><pub>Elsevier</pub><pmid>9712689</pmid><doi>10.1006/mpat.1998.0216</doi><tpages>9</tpages></addata></record> |
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| ispartof | Microbial pathogenesis, 1998-08, Vol.25 (2), p.101-109 |
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| subjects | Amino Acid Sequence Animals Antibodies, Monoclonal Antigens, Bacterial - chemistry Antigens, Bacterial - genetics Antigens, Bacterial - immunology Antigens, Surface - chemistry Antigens, Surface - genetics Antigens, Surface - immunology Bacterial Proteins Bacteriology Biological and medical sciences Erysipelothrix - classification Erysipelothrix - genetics Erysipelothrix - immunology Erysipelothrix rhusiopathiae Escherichia coli - immunology Escherichia coli - physiology Fundamental and applied biological sciences. Psychology Genes, Bacterial Humans Mice Microbiology Molecular Sequence Data Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Sequence Alignment Sequence Deletion Sequence Homology, Amino Acid Serotyping Swine Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies |
| title | Properties of repeat domain found in a novel protective antigen, SpaA, of Erysipelothrix rhusiopathiae |
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