The fibronectin‐binding protein homologue Fbp62 of Streptococcus anginosus is a potent virulence factor
ABSTRACT Streptococcus anginosus appears to be able to adhere to cultured epithelial cells or fibronectin and this may be associated with bacterial pathogenicity. In the present study, the molecular characteristics and virulence of the fibronectin‐binding protein (FBP), Fbp62, of S. anginosus were i...
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| Veröffentlicht in: | Microbiology and immunology 2018-10, Vol.62 (10), p.624-634 |
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| creator | Kodama, Yoshitoyo Ishikawa, Taichi Shimoyama, Yu Sasaki, Daisuke Kimura, Shigenobu Sasaki, Minoru |
| description | ABSTRACT
Streptococcus anginosus appears to be able to adhere to cultured epithelial cells or fibronectin and this may be associated with bacterial pathogenicity. In the present study, the molecular characteristics and virulence of the fibronectin‐binding protein (FBP), Fbp62, of S. anginosus were investigated in animal models to determine the role of the molecule in bacterial infection. fbp62 encodes a 549 amino acid residue with an apparent molecular mass of 62.8 kDa that lacks a membrane anchor motif and a leader peptide, suggesting that fbp62 codes for an atypical FBP. It has been observed that the S. anginosus Fbp62 is very similar to the FbpA of Streptococcus gordonii, PavA of Streptococcus pneumoniae, SmFnB of Streptococcus mutans and Fbp54 of Streptococcus pyogenes. Recombinant Fbp62 prepared from pGEX‐4T‐2 was found to bind to fibronectin in a dose‐dependent manner and competitively inhibit the binding of S. anginosus to fibronectin. Furthermore, anti‐Fbp62 antiserum abrogated the binding of S. anginosus to fibronectin. Adhesion of the isogenic mutant, Δfbp62, constructed from S. anginosus NCTC 10713 (wild‐type, WT) by homologous recombination to HEp‐2 cells and DOK cells was significantly weaker than that of S. anginosus WT. In addition, Δfbp62’s lethality and ability to form abscesses were weaker in a mouse model of infection than in the WT strain. Taken together, these results suggest that Fbp62 is an important pathogenic factor of S. anginosus. |
| doi_str_mv | 10.1111/1348-0421.12646 |
| format | Article |
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Streptococcus anginosus appears to be able to adhere to cultured epithelial cells or fibronectin and this may be associated with bacterial pathogenicity. In the present study, the molecular characteristics and virulence of the fibronectin‐binding protein (FBP), Fbp62, of S. anginosus were investigated in animal models to determine the role of the molecule in bacterial infection. fbp62 encodes a 549 amino acid residue with an apparent molecular mass of 62.8 kDa that lacks a membrane anchor motif and a leader peptide, suggesting that fbp62 codes for an atypical FBP. It has been observed that the S. anginosus Fbp62 is very similar to the FbpA of Streptococcus gordonii, PavA of Streptococcus pneumoniae, SmFnB of Streptococcus mutans and Fbp54 of Streptococcus pyogenes. Recombinant Fbp62 prepared from pGEX‐4T‐2 was found to bind to fibronectin in a dose‐dependent manner and competitively inhibit the binding of S. anginosus to fibronectin. Furthermore, anti‐Fbp62 antiserum abrogated the binding of S. anginosus to fibronectin. Adhesion of the isogenic mutant, Δfbp62, constructed from S. anginosus NCTC 10713 (wild‐type, WT) by homologous recombination to HEp‐2 cells and DOK cells was significantly weaker than that of S. anginosus WT. In addition, Δfbp62’s lethality and ability to form abscesses were weaker in a mouse model of infection than in the WT strain. Taken together, these results suggest that Fbp62 is an important pathogenic factor of S. anginosus.</description><identifier>ISSN: 0385-5600</identifier><identifier>EISSN: 1348-0421</identifier><identifier>DOI: 10.1111/1348-0421.12646</identifier><identifier>PMID: 30192020</identifier><language>eng</language><publisher>Australia: Wiley Subscription Services, Inc</publisher><subject>Abscesses ; Adhesins, Bacterial - genetics ; Adhesins, Bacterial - immunology ; Animal models ; Animals ; Bacterial Adhesion ; Bacterial infections ; Bacterial Outer Membrane Proteins - genetics ; Bacterial Outer Membrane Proteins - metabolism ; Bacterial Proteins - genetics ; Bacterial Proteins - immunology ; Bacterial Proteins - metabolism ; Carrier Proteins - metabolism ; Cell Line ; Disease Models, Animal ; Epithelial Cells ; Fibronectin ; Fibronectins - metabolism ; fibronectin‐binding protein ; Genes, Bacterial ; Hep G2 Cells ; Homologous recombination ; Homology ; Humans ; Infections ; Lethality ; Male ; Mice ; Mice, Inbred BALB C ; Pathogenicity ; Pathogens ; Protein sorting signals ; Recombinant Proteins - immunology ; S. anginosus ; Streptococcus anginosus ; Streptococcus anginosus - genetics ; Streptococcus anginosus - immunology ; Streptococcus anginosus - metabolism ; Streptococcus anginosus - pathogenicity ; Streptococcus gordonii - metabolism ; Streptococcus infections ; Streptococcus mutans - metabolism ; Streptococcus pneumoniae - immunology ; Streptococcus pyogenes - metabolism ; Virulence ; virulence factor ; Virulence factors ; Virulence Factors - immunology</subject><ispartof>Microbiology and immunology, 2018-10, Vol.62 (10), p.624-634</ispartof><rights>2018 The Societies and John Wiley & Sons Australia, Ltd</rights><rights>2018 The Societies and John Wiley & Sons Australia, Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5296-5f371c8abc72b719770f326662da7c84986422613dbfa2bd97118cf9eaa35f4c3</citedby><cites>FETCH-LOGICAL-c5296-5f371c8abc72b719770f326662da7c84986422613dbfa2bd97118cf9eaa35f4c3</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%2F1348-0421.12646$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2F1348-0421.12646$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30192020$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kodama, Yoshitoyo</creatorcontrib><creatorcontrib>Ishikawa, Taichi</creatorcontrib><creatorcontrib>Shimoyama, Yu</creatorcontrib><creatorcontrib>Sasaki, Daisuke</creatorcontrib><creatorcontrib>Kimura, Shigenobu</creatorcontrib><creatorcontrib>Sasaki, Minoru</creatorcontrib><title>The fibronectin‐binding protein homologue Fbp62 of Streptococcus anginosus is a potent virulence factor</title><title>Microbiology and immunology</title><addtitle>Microbiol Immunol</addtitle><description>ABSTRACT
Streptococcus anginosus appears to be able to adhere to cultured epithelial cells or fibronectin and this may be associated with bacterial pathogenicity. In the present study, the molecular characteristics and virulence of the fibronectin‐binding protein (FBP), Fbp62, of S. anginosus were investigated in animal models to determine the role of the molecule in bacterial infection. fbp62 encodes a 549 amino acid residue with an apparent molecular mass of 62.8 kDa that lacks a membrane anchor motif and a leader peptide, suggesting that fbp62 codes for an atypical FBP. It has been observed that the S. anginosus Fbp62 is very similar to the FbpA of Streptococcus gordonii, PavA of Streptococcus pneumoniae, SmFnB of Streptococcus mutans and Fbp54 of Streptococcus pyogenes. Recombinant Fbp62 prepared from pGEX‐4T‐2 was found to bind to fibronectin in a dose‐dependent manner and competitively inhibit the binding of S. anginosus to fibronectin. Furthermore, anti‐Fbp62 antiserum abrogated the binding of S. anginosus to fibronectin. Adhesion of the isogenic mutant, Δfbp62, constructed from S. anginosus NCTC 10713 (wild‐type, WT) by homologous recombination to HEp‐2 cells and DOK cells was significantly weaker than that of S. anginosus WT. In addition, Δfbp62’s lethality and ability to form abscesses were weaker in a mouse model of infection than in the WT strain. Taken together, these results suggest that Fbp62 is an important pathogenic factor of S. anginosus.</description><subject>Abscesses</subject><subject>Adhesins, Bacterial - genetics</subject><subject>Adhesins, Bacterial - immunology</subject><subject>Animal models</subject><subject>Animals</subject><subject>Bacterial Adhesion</subject><subject>Bacterial infections</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - immunology</subject><subject>Bacterial Proteins - metabolism</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Line</subject><subject>Disease Models, Animal</subject><subject>Epithelial Cells</subject><subject>Fibronectin</subject><subject>Fibronectins - metabolism</subject><subject>fibronectin‐binding protein</subject><subject>Genes, Bacterial</subject><subject>Hep G2 Cells</subject><subject>Homologous recombination</subject><subject>Homology</subject><subject>Humans</subject><subject>Infections</subject><subject>Lethality</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Pathogenicity</subject><subject>Pathogens</subject><subject>Protein sorting signals</subject><subject>Recombinant Proteins - immunology</subject><subject>S. anginosus</subject><subject>Streptococcus anginosus</subject><subject>Streptococcus anginosus - genetics</subject><subject>Streptococcus anginosus - immunology</subject><subject>Streptococcus anginosus - metabolism</subject><subject>Streptococcus anginosus - pathogenicity</subject><subject>Streptococcus gordonii - metabolism</subject><subject>Streptococcus infections</subject><subject>Streptococcus mutans - metabolism</subject><subject>Streptococcus pneumoniae - immunology</subject><subject>Streptococcus pyogenes - metabolism</subject><subject>Virulence</subject><subject>virulence factor</subject><subject>Virulence factors</subject><subject>Virulence Factors - immunology</subject><issn>0385-5600</issn><issn>1348-0421</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFOHSEUhknTpt7art0Zkm7cjMKBAWZpTG1NNF3UrgnDwBUzF0aYsXHnI_iMPkm5vdZFN2UDh3zny8l_EDqg5JjWc0IZVw3hQI8pCC7eoNXrz1u0Iky1TSsI2UMfSrklBCQo_h7tMUI7IEBWKFzfOOxDn1N0dg7x-fGpD3EIcY2nnGYXIr5JmzSm9eLweT8JwMnjH3N205xssnYp2MR1iKnUV6gFnmpbnPF9yMvooq16Y-eUP6J33ozFfXq599HP8y_XZ9-ay-9fL85OLxvbQiea1jNJrTK9ldBL2klJPAMhBAxGWsU7JTiAoGzovYF-6CSlyvrOGcNazy3bR0c7b53_bnFl1ptQrBtHE11aigZKKEihJK3o53_Q27TkWKerFLBWKk55pU52lM2plOy8nnLYmPygKdHbLeht5nqbuf6zhdpx-OJd-o0bXvm_sVeg3QG_wuge_ufTVxdXO_Fvo-qR8w</recordid><startdate>201810</startdate><enddate>201810</enddate><creator>Kodama, Yoshitoyo</creator><creator>Ishikawa, Taichi</creator><creator>Shimoyama, Yu</creator><creator>Sasaki, Daisuke</creator><creator>Kimura, Shigenobu</creator><creator>Sasaki, Minoru</creator><general>Wiley Subscription Services, Inc</general><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>7T5</scope><scope>7U9</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>201810</creationdate><title>The fibronectin‐binding protein homologue Fbp62 of Streptococcus anginosus is a potent virulence factor</title><author>Kodama, Yoshitoyo ; Ishikawa, Taichi ; Shimoyama, Yu ; Sasaki, Daisuke ; Kimura, Shigenobu ; Sasaki, Minoru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5296-5f371c8abc72b719770f326662da7c84986422613dbfa2bd97118cf9eaa35f4c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Abscesses</topic><topic>Adhesins, Bacterial - genetics</topic><topic>Adhesins, Bacterial - immunology</topic><topic>Animal models</topic><topic>Animals</topic><topic>Bacterial Adhesion</topic><topic>Bacterial infections</topic><topic>Bacterial Outer Membrane Proteins - genetics</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - immunology</topic><topic>Bacterial Proteins - metabolism</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Line</topic><topic>Disease Models, Animal</topic><topic>Epithelial Cells</topic><topic>Fibronectin</topic><topic>Fibronectins - metabolism</topic><topic>fibronectin‐binding protein</topic><topic>Genes, Bacterial</topic><topic>Hep G2 Cells</topic><topic>Homologous recombination</topic><topic>Homology</topic><topic>Humans</topic><topic>Infections</topic><topic>Lethality</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Pathogenicity</topic><topic>Pathogens</topic><topic>Protein sorting signals</topic><topic>Recombinant Proteins - immunology</topic><topic>S. anginosus</topic><topic>Streptococcus anginosus</topic><topic>Streptococcus anginosus - genetics</topic><topic>Streptococcus anginosus - immunology</topic><topic>Streptococcus anginosus - metabolism</topic><topic>Streptococcus anginosus - pathogenicity</topic><topic>Streptococcus gordonii - metabolism</topic><topic>Streptococcus infections</topic><topic>Streptococcus mutans - metabolism</topic><topic>Streptococcus pneumoniae - immunology</topic><topic>Streptococcus pyogenes - metabolism</topic><topic>Virulence</topic><topic>virulence factor</topic><topic>Virulence factors</topic><topic>Virulence Factors - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kodama, Yoshitoyo</creatorcontrib><creatorcontrib>Ishikawa, Taichi</creatorcontrib><creatorcontrib>Shimoyama, Yu</creatorcontrib><creatorcontrib>Sasaki, Daisuke</creatorcontrib><creatorcontrib>Kimura, Shigenobu</creatorcontrib><creatorcontrib>Sasaki, Minoru</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Microbiology and immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kodama, Yoshitoyo</au><au>Ishikawa, Taichi</au><au>Shimoyama, Yu</au><au>Sasaki, Daisuke</au><au>Kimura, Shigenobu</au><au>Sasaki, Minoru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The fibronectin‐binding protein homologue Fbp62 of Streptococcus anginosus is a potent virulence factor</atitle><jtitle>Microbiology and immunology</jtitle><addtitle>Microbiol Immunol</addtitle><date>2018-10</date><risdate>2018</risdate><volume>62</volume><issue>10</issue><spage>624</spage><epage>634</epage><pages>624-634</pages><issn>0385-5600</issn><eissn>1348-0421</eissn><abstract>ABSTRACT
Streptococcus anginosus appears to be able to adhere to cultured epithelial cells or fibronectin and this may be associated with bacterial pathogenicity. In the present study, the molecular characteristics and virulence of the fibronectin‐binding protein (FBP), Fbp62, of S. anginosus were investigated in animal models to determine the role of the molecule in bacterial infection. fbp62 encodes a 549 amino acid residue with an apparent molecular mass of 62.8 kDa that lacks a membrane anchor motif and a leader peptide, suggesting that fbp62 codes for an atypical FBP. It has been observed that the S. anginosus Fbp62 is very similar to the FbpA of Streptococcus gordonii, PavA of Streptococcus pneumoniae, SmFnB of Streptococcus mutans and Fbp54 of Streptococcus pyogenes. Recombinant Fbp62 prepared from pGEX‐4T‐2 was found to bind to fibronectin in a dose‐dependent manner and competitively inhibit the binding of S. anginosus to fibronectin. Furthermore, anti‐Fbp62 antiserum abrogated the binding of S. anginosus to fibronectin. Adhesion of the isogenic mutant, Δfbp62, constructed from S. anginosus NCTC 10713 (wild‐type, WT) by homologous recombination to HEp‐2 cells and DOK cells was significantly weaker than that of S. anginosus WT. In addition, Δfbp62’s lethality and ability to form abscesses were weaker in a mouse model of infection than in the WT strain. Taken together, these results suggest that Fbp62 is an important pathogenic factor of S. anginosus.</abstract><cop>Australia</cop><pub>Wiley Subscription Services, Inc</pub><pmid>30192020</pmid><doi>10.1111/1348-0421.12646</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Microbiology and immunology, 2018-10, Vol.62 (10), p.624-634 |
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| source | Freely Accessible Japanese Titles (ERDB Project); MEDLINE; Wiley Online Library Journals; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Abscesses Adhesins, Bacterial - genetics Adhesins, Bacterial - immunology Animal models Animals Bacterial Adhesion Bacterial infections Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Bacterial Proteins - genetics Bacterial Proteins - immunology Bacterial Proteins - metabolism Carrier Proteins - metabolism Cell Line Disease Models, Animal Epithelial Cells Fibronectin Fibronectins - metabolism fibronectin‐binding protein Genes, Bacterial Hep G2 Cells Homologous recombination Homology Humans Infections Lethality Male Mice Mice, Inbred BALB C Pathogenicity Pathogens Protein sorting signals Recombinant Proteins - immunology S. anginosus Streptococcus anginosus Streptococcus anginosus - genetics Streptococcus anginosus - immunology Streptococcus anginosus - metabolism Streptococcus anginosus - pathogenicity Streptococcus gordonii - metabolism Streptococcus infections Streptococcus mutans - metabolism Streptococcus pneumoniae - immunology Streptococcus pyogenes - metabolism Virulence virulence factor Virulence factors Virulence Factors - immunology |
| title | The fibronectin‐binding protein homologue Fbp62 of Streptococcus anginosus is a potent virulence factor |
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