Analysis of the expression of the putatively virulence-associated neisserial protein RmpM (class 4) in commensal Neisseria and Moraxella catarrhalis strains
Abstract The RmpM protein has been reported to be present only in pathogenic Neisseria species. In the present study we demonstrate that this protein is also present at least in N. lactamica and N. sicca strains. The N. lactamica protein reacts with a RmpM-specific monoclonal antibody (185, H-8), ha...
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| Veröffentlicht in: | FEMS microbiology letters 2001-05, Vol.199 (2), p.171-176 |
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| creator | Troncoso, Gemma Sánchez, Sandra Kolberg, Jan Rosenqvist, Einar Veiga, Manuel Ferreirós, Carlos M. Criado, María- |
| description | Abstract
The RmpM protein has been reported to be present only in pathogenic Neisseria species. In the present study we demonstrate that this protein is also present at least in N. lactamica and N. sicca strains. The N. lactamica protein reacts with a RmpM-specific monoclonal antibody (185, H-8), having a molecular mass (∼31 kDa) slightly lower than that of the meningococcal RmpM, and mouse antibodies from sera against outer membrane vesicles from both N. lactamica and N. sicca strains cross-react with the meningococcal RmpM. PCR and hybridization experiments with a complete rmpM probe agree with the immunodetection experiments. Our results strongly suggest that the meningococcal RmpM should not be considered a virulence marker, and the presence of this protein in the commensal species agrees with its role as a structural protein, proposed for the RmpM, which should be considerably conserved in the Neisseria species. |
| doi_str_mv | 10.1111/j.1574-6968.2001.tb10669.x |
| format | Article |
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The RmpM protein has been reported to be present only in pathogenic Neisseria species. In the present study we demonstrate that this protein is also present at least in N. lactamica and N. sicca strains. The N. lactamica protein reacts with a RmpM-specific monoclonal antibody (185, H-8), having a molecular mass (∼31 kDa) slightly lower than that of the meningococcal RmpM, and mouse antibodies from sera against outer membrane vesicles from both N. lactamica and N. sicca strains cross-react with the meningococcal RmpM. PCR and hybridization experiments with a complete rmpM probe agree with the immunodetection experiments. Our results strongly suggest that the meningococcal RmpM should not be considered a virulence marker, and the presence of this protein in the commensal species agrees with its role as a structural protein, proposed for the RmpM, which should be considerably conserved in the Neisseria species.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2001.tb10669.x</identifier><identifier>PMID: 11377862</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Antibodies, Monoclonal - immunology ; Antigens, Bacterial - analysis ; Antigens, Bacterial - physiology ; Bacterial Outer Membrane Proteins - analysis ; Bacterial Outer Membrane Proteins - physiology ; Bacterial Proteins - analysis ; Bacterial Proteins - physiology ; Bacteriology ; Biological and medical sciences ; Class 4 protein ; Commensal Neisseria ; Fundamental and applied biological sciences. Psychology ; Genetics ; Hybridization ; Membrane vesicles ; Microbiology ; Molecular Weight ; Monoclonal antibodies ; Moraxella (Branhamella) catarrhalis - metabolism ; Moraxella (Branhamella) catarrhalis - pathogenicity ; Moraxella catarrhalis ; Neisseria ; Neisseria - metabolism ; Neisseria - pathogenicity ; Neisseria meningitidis ; Notiphila sicca ; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains ; Proteins ; RmpM ; RmpM protein ; Species ; Virulence</subject><ispartof>FEMS microbiology letters, 2001-05, Vol.199 (2), p.171-176</ispartof><rights>2001 Federation of European Microbiological Societies 2001</rights><rights>2002 INIST-CNRS</rights><rights>2001 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4041-42da10230f89d4a09e822de3cbcff2f9dd1b3e6ccd534b438cf76f41c6a4e9093</citedby><cites>FETCH-LOGICAL-c4041-42da10230f89d4a09e822de3cbcff2f9dd1b3e6ccd534b438cf76f41c6a4e9093</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.1574-6968.2001.tb10669.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2001.tb10669.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14164847$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11377862$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Troncoso, Gemma</creatorcontrib><creatorcontrib>Sánchez, Sandra</creatorcontrib><creatorcontrib>Kolberg, Jan</creatorcontrib><creatorcontrib>Rosenqvist, Einar</creatorcontrib><creatorcontrib>Veiga, Manuel</creatorcontrib><creatorcontrib>Ferreirós, Carlos M.</creatorcontrib><creatorcontrib>Criado, María-</creatorcontrib><title>Analysis of the expression of the putatively virulence-associated neisserial protein RmpM (class 4) in commensal Neisseria and Moraxella catarrhalis strains</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
The RmpM protein has been reported to be present only in pathogenic Neisseria species. In the present study we demonstrate that this protein is also present at least in N. lactamica and N. sicca strains. The N. lactamica protein reacts with a RmpM-specific monoclonal antibody (185, H-8), having a molecular mass (∼31 kDa) slightly lower than that of the meningococcal RmpM, and mouse antibodies from sera against outer membrane vesicles from both N. lactamica and N. sicca strains cross-react with the meningococcal RmpM. PCR and hybridization experiments with a complete rmpM probe agree with the immunodetection experiments. Our results strongly suggest that the meningococcal RmpM should not be considered a virulence marker, and the presence of this protein in the commensal species agrees with its role as a structural protein, proposed for the RmpM, which should be considerably conserved in the Neisseria species.</description><subject>Antibodies, Monoclonal - immunology</subject><subject>Antigens, Bacterial - analysis</subject><subject>Antigens, Bacterial - physiology</subject><subject>Bacterial Outer Membrane Proteins - analysis</subject><subject>Bacterial Outer Membrane Proteins - physiology</subject><subject>Bacterial Proteins - analysis</subject><subject>Bacterial Proteins - physiology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Class 4 protein</subject><subject>Commensal Neisseria</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetics</subject><subject>Hybridization</subject><subject>Membrane vesicles</subject><subject>Microbiology</subject><subject>Molecular Weight</subject><subject>Monoclonal antibodies</subject><subject>Moraxella (Branhamella) catarrhalis - metabolism</subject><subject>Moraxella (Branhamella) catarrhalis - pathogenicity</subject><subject>Moraxella catarrhalis</subject><subject>Neisseria</subject><subject>Neisseria - metabolism</subject><subject>Neisseria - pathogenicity</subject><subject>Neisseria meningitidis</subject><subject>Notiphila sicca</subject><subject>Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains</subject><subject>Proteins</subject><subject>RmpM</subject><subject>RmpM protein</subject><subject>Species</subject><subject>Virulence</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</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>eNqVkV-LEzEUxQdR3O7qV5CgKPowNXcmnSQ-CMviqtAqiD6HNHOHTcn8MXdmbb_LflhT2nVBFDEvgZvfOTnJybKnwOeQ1uvNHBZS5JWu1LzgHObjGnhV6fn2Xjb7dXQ_m_FSqhy4lifZKdGGcy4KXj3MTgBKKVVVzLKb886GHXlifcPGK2S4HSIS-b67nQzTaEd_jWHHrn2cAnYOc0vUO29HrFmHngijt4ENsR_Rd-xLO6zYSxcSxcQrliaub1vsKDGfbnFmu5qt-mi3GIJlzo42xisbUhYao_UdPcoeNDYQPj7uZ9m3y3dfLz7ky8_vP16cL3MnuIBcFLUFXpS8UboWlmtURVFj6dauaYpG1zWsS6ycqxelWItSuUZWjQBXWYGa6_Ise3HwTfm_T0ijaT25faoO-4mM5JoLJct_giCVAs0XCXz2G7jpp5i-mkxRAvCF1KAS9eZAudgTRWzMEH1r484AN_uqzcbs-zT7Ps2-anOs2myT-MnximndYn0nPXabgOdHwJKzoYm2c57uOAGVUEIm7u2B--ED7v4jgrlcLUFCMlgcDPpp-Is8_9MLfgLhi9jc</recordid><startdate>200105</startdate><enddate>200105</enddate><creator>Troncoso, Gemma</creator><creator>Sánchez, Sandra</creator><creator>Kolberg, Jan</creator><creator>Rosenqvist, Einar</creator><creator>Veiga, Manuel</creator><creator>Ferreirós, Carlos M.</creator><creator>Criado, María-</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>200105</creationdate><title>Analysis of the expression of the putatively virulence-associated neisserial protein RmpM (class 4) in commensal Neisseria and Moraxella catarrhalis strains</title><author>Troncoso, Gemma ; Sánchez, Sandra ; Kolberg, Jan ; Rosenqvist, Einar ; Veiga, Manuel ; Ferreirós, Carlos M. ; Criado, María-</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4041-42da10230f89d4a09e822de3cbcff2f9dd1b3e6ccd534b438cf76f41c6a4e9093</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Antibodies, Monoclonal - immunology</topic><topic>Antigens, Bacterial - analysis</topic><topic>Antigens, Bacterial - physiology</topic><topic>Bacterial Outer Membrane Proteins - analysis</topic><topic>Bacterial Outer Membrane Proteins - physiology</topic><topic>Bacterial Proteins - analysis</topic><topic>Bacterial Proteins - physiology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Class 4 protein</topic><topic>Commensal Neisseria</topic><topic>Fundamental and applied biological sciences. 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The RmpM protein has been reported to be present only in pathogenic Neisseria species. In the present study we demonstrate that this protein is also present at least in N. lactamica and N. sicca strains. The N. lactamica protein reacts with a RmpM-specific monoclonal antibody (185, H-8), having a molecular mass (∼31 kDa) slightly lower than that of the meningococcal RmpM, and mouse antibodies from sera against outer membrane vesicles from both N. lactamica and N. sicca strains cross-react with the meningococcal RmpM. PCR and hybridization experiments with a complete rmpM probe agree with the immunodetection experiments. Our results strongly suggest that the meningococcal RmpM should not be considered a virulence marker, and the presence of this protein in the commensal species agrees with its role as a structural protein, proposed for the RmpM, which should be considerably conserved in the Neisseria species.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>11377862</pmid><doi>10.1111/j.1574-6968.2001.tb10669.x</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEMS microbiology letters, 2001-05, Vol.199 (2), p.171-176 |
| issn | 0378-1097 1574-6968 |
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| subjects | Antibodies, Monoclonal - immunology Antigens, Bacterial - analysis Antigens, Bacterial - physiology Bacterial Outer Membrane Proteins - analysis Bacterial Outer Membrane Proteins - physiology Bacterial Proteins - analysis Bacterial Proteins - physiology Bacteriology Biological and medical sciences Class 4 protein Commensal Neisseria Fundamental and applied biological sciences. Psychology Genetics Hybridization Membrane vesicles Microbiology Molecular Weight Monoclonal antibodies Moraxella (Branhamella) catarrhalis - metabolism Moraxella (Branhamella) catarrhalis - pathogenicity Moraxella catarrhalis Neisseria Neisseria - metabolism Neisseria - pathogenicity Neisseria meningitidis Notiphila sicca Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Proteins RmpM RmpM protein Species Virulence |
| title | Analysis of the expression of the putatively virulence-associated neisserial protein RmpM (class 4) in commensal Neisseria and Moraxella catarrhalis strains |
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