Glucan Binding Protein C of Streptococcus mutans Mediates both Sucrose-Independent and Sucrose-Dependent Adherence
The high-resolution structure of glucan binding protein C (GbpC) at 1.14 Å, a sucrose-dependent virulence factor of the dental caries pathogen , has been determined. GbpC shares not only structural similarities with the V regions of AgI/II and SspB but also functional adherence to salivary agglutini...
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| Veröffentlicht in: | Infection and immunity 2018-07, Vol.86 (7) |
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| creator | Mieher, Joshua L Larson, Matthew R Schormann, Norbert Purushotham, Sangeetha Wu, Ren Rajashankar, Kanagalaghatta R Wu, Hui Deivanayagam, Champion |
| description | The high-resolution structure of glucan binding protein C (GbpC) at 1.14 Å, a sucrose-dependent virulence factor of the dental caries pathogen
, has been determined. GbpC shares not only structural similarities with the V regions of AgI/II and SspB but also functional adherence to salivary agglutinin (SAG) and its scavenger receptor cysteine-rich domains (SRCRs). This is not only a newly identified function for GbpC but also an additional fail-safe binding mechanism for
Despite the structural similarities with
antigen I/II (AgI/II) and SspB of
, GbpC remains unique among these surface proteins in its propensity to adhere to dextran/glucans. The complex crystal structure of GbpC with dextrose (β-d-glucose; Protein Data Bank ligand BGC) highlights exclusive structural features that facilitate this interaction with dextran. Targeted deletion mutant studies on GbpC's divergent loop region in the vicinity of a highly conserved calcium binding site confirm its role in biofilm formation. Finally, we present a model for adherence to dextran. The structure of GbpC highlights how artfully microbes have engineered the lectin-like folds to broaden their functional adherence repertoire. |
| doi_str_mv | 10.1128/IAI.00146-18 |
| format | Article |
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, has been determined. GbpC shares not only structural similarities with the V regions of AgI/II and SspB but also functional adherence to salivary agglutinin (SAG) and its scavenger receptor cysteine-rich domains (SRCRs). This is not only a newly identified function for GbpC but also an additional fail-safe binding mechanism for
Despite the structural similarities with
antigen I/II (AgI/II) and SspB of
, GbpC remains unique among these surface proteins in its propensity to adhere to dextran/glucans. The complex crystal structure of GbpC with dextrose (β-d-glucose; Protein Data Bank ligand BGC) highlights exclusive structural features that facilitate this interaction with dextran. Targeted deletion mutant studies on GbpC's divergent loop region in the vicinity of a highly conserved calcium binding site confirm its role in biofilm formation. Finally, we present a model for adherence to dextran. The structure of GbpC highlights how artfully microbes have engineered the lectin-like folds to broaden their functional adherence repertoire.</description><identifier>ISSN: 0019-9567</identifier><identifier>EISSN: 1098-5522</identifier><identifier>DOI: 10.1128/IAI.00146-18</identifier><identifier>PMID: 29685986</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Bacterial Adhesion ; Biofilms ; Calcium-Binding Proteins ; Carrier Proteins - chemistry ; Carrier Proteins - physiology ; Crystallography ; Dextrans - chemistry ; DNA-Binding Proteins ; Lectins - chemistry ; Lectins - physiology ; Molecular Pathogenesis ; Receptors, Cell Surface - chemistry ; Receptors, Scavenger - chemistry ; Streptococcus mutans - physiology ; Sucrose - pharmacology ; Tumor Suppressor Proteins</subject><ispartof>Infection and immunity, 2018-07, Vol.86 (7)</ispartof><rights>Copyright © 2018 American Society for Microbiology.</rights><rights>Copyright © 2018 American Society for Microbiology. 2018 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-de9cd38128b5b4c927f65ac274d63d9143dd3aa6f43bec55f11f85d3f7b63d153</citedby><cites>FETCH-LOGICAL-c520t-de9cd38128b5b4c927f65ac274d63d9143dd3aa6f43bec55f11f85d3f7b63d153</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/PMC6013656/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6013656/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,3175,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29685986$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1460844$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Mieher, Joshua L</creatorcontrib><creatorcontrib>Larson, Matthew R</creatorcontrib><creatorcontrib>Schormann, Norbert</creatorcontrib><creatorcontrib>Purushotham, Sangeetha</creatorcontrib><creatorcontrib>Wu, Ren</creatorcontrib><creatorcontrib>Rajashankar, Kanagalaghatta R</creatorcontrib><creatorcontrib>Wu, Hui</creatorcontrib><creatorcontrib>Deivanayagam, Champion</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Glucan Binding Protein C of Streptococcus mutans Mediates both Sucrose-Independent and Sucrose-Dependent Adherence</title><title>Infection and immunity</title><addtitle>Infect Immun</addtitle><description>The high-resolution structure of glucan binding protein C (GbpC) at 1.14 Å, a sucrose-dependent virulence factor of the dental caries pathogen
, has been determined. GbpC shares not only structural similarities with the V regions of AgI/II and SspB but also functional adherence to salivary agglutinin (SAG) and its scavenger receptor cysteine-rich domains (SRCRs). This is not only a newly identified function for GbpC but also an additional fail-safe binding mechanism for
Despite the structural similarities with
antigen I/II (AgI/II) and SspB of
, GbpC remains unique among these surface proteins in its propensity to adhere to dextran/glucans. The complex crystal structure of GbpC with dextrose (β-d-glucose; Protein Data Bank ligand BGC) highlights exclusive structural features that facilitate this interaction with dextran. Targeted deletion mutant studies on GbpC's divergent loop region in the vicinity of a highly conserved calcium binding site confirm its role in biofilm formation. Finally, we present a model for adherence to dextran. The structure of GbpC highlights how artfully microbes have engineered the lectin-like folds to broaden their functional adherence repertoire.</description><subject>Bacterial Adhesion</subject><subject>Biofilms</subject><subject>Calcium-Binding Proteins</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - physiology</subject><subject>Crystallography</subject><subject>Dextrans - chemistry</subject><subject>DNA-Binding Proteins</subject><subject>Lectins - chemistry</subject><subject>Lectins - physiology</subject><subject>Molecular Pathogenesis</subject><subject>Receptors, Cell Surface - chemistry</subject><subject>Receptors, Scavenger - chemistry</subject><subject>Streptococcus mutans - physiology</subject><subject>Sucrose - pharmacology</subject><subject>Tumor Suppressor Proteins</subject><issn>0019-9567</issn><issn>1098-5522</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkc1vEzEUxC0EomnhxhlZnDh0i7_jvSCFACVSEUiFs-W13zZGGzu1vUj89zikRHCxpXk_jcdvEHpByRWlTL_ZrDZXhFChOqofoQUlve6kZOwxWjS573qplmfovJQfB0oI_RSdsV5p2Wu1QPl6mp2N-F2IPsQ7_DWnCiHiNU4jvq0Z9jW55Nxc8G6uNhb8GXywFQoeUt3i29nlVKDbRA97aEes2EZ_0t-f1JXfQobo4Bl6MtqpwPOH-wJ9__jh2_pTd_PlerNe3XROMlI7D73zXLcvDnIQrmfLUUnr2FJ4xX1PBfeeW6tGwQdwUo6Ujlp6Pi6HNqeSX6C3R9_9POzAuxYi28nsc9jZ_MskG8z_kxi25i79NIpQrqRqBq-OBqnUYIoLFdzWpRjBVdMWTrQQDXr98EpO9zOUanahOJgmGyHNxTDCKWGS6QN6eUQPqykZxlMWSsyhS9O6NH-6NFQ3_OW_-U_w3_L4b5xcm-A</recordid><startdate>20180701</startdate><enddate>20180701</enddate><creator>Mieher, Joshua L</creator><creator>Larson, Matthew R</creator><creator>Schormann, Norbert</creator><creator>Purushotham, Sangeetha</creator><creator>Wu, Ren</creator><creator>Rajashankar, Kanagalaghatta R</creator><creator>Wu, Hui</creator><creator>Deivanayagam, Champion</creator><general>American Society for Microbiology</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>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20180701</creationdate><title>Glucan Binding Protein C of Streptococcus mutans Mediates both Sucrose-Independent and Sucrose-Dependent Adherence</title><author>Mieher, Joshua L ; Larson, Matthew R ; Schormann, Norbert ; Purushotham, Sangeetha ; Wu, Ren ; Rajashankar, Kanagalaghatta R ; Wu, Hui ; Deivanayagam, Champion</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c520t-de9cd38128b5b4c927f65ac274d63d9143dd3aa6f43bec55f11f85d3f7b63d153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Bacterial Adhesion</topic><topic>Biofilms</topic><topic>Calcium-Binding Proteins</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - physiology</topic><topic>Crystallography</topic><topic>Dextrans - chemistry</topic><topic>DNA-Binding Proteins</topic><topic>Lectins - chemistry</topic><topic>Lectins - physiology</topic><topic>Molecular Pathogenesis</topic><topic>Receptors, Cell Surface - chemistry</topic><topic>Receptors, Scavenger - chemistry</topic><topic>Streptococcus mutans - physiology</topic><topic>Sucrose - pharmacology</topic><topic>Tumor Suppressor Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mieher, Joshua L</creatorcontrib><creatorcontrib>Larson, Matthew R</creatorcontrib><creatorcontrib>Schormann, Norbert</creatorcontrib><creatorcontrib>Purushotham, Sangeetha</creatorcontrib><creatorcontrib>Wu, Ren</creatorcontrib><creatorcontrib>Rajashankar, Kanagalaghatta R</creatorcontrib><creatorcontrib>Wu, Hui</creatorcontrib><creatorcontrib>Deivanayagam, Champion</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><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>OSTI.GOV</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>Mieher, Joshua L</au><au>Larson, Matthew R</au><au>Schormann, Norbert</au><au>Purushotham, Sangeetha</au><au>Wu, Ren</au><au>Rajashankar, Kanagalaghatta R</au><au>Wu, Hui</au><au>Deivanayagam, Champion</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glucan Binding Protein C of Streptococcus mutans Mediates both Sucrose-Independent and Sucrose-Dependent Adherence</atitle><jtitle>Infection and immunity</jtitle><addtitle>Infect Immun</addtitle><date>2018-07-01</date><risdate>2018</risdate><volume>86</volume><issue>7</issue><issn>0019-9567</issn><eissn>1098-5522</eissn><abstract>The high-resolution structure of glucan binding protein C (GbpC) at 1.14 Å, a sucrose-dependent virulence factor of the dental caries pathogen
, has been determined. GbpC shares not only structural similarities with the V regions of AgI/II and SspB but also functional adherence to salivary agglutinin (SAG) and its scavenger receptor cysteine-rich domains (SRCRs). This is not only a newly identified function for GbpC but also an additional fail-safe binding mechanism for
Despite the structural similarities with
antigen I/II (AgI/II) and SspB of
, GbpC remains unique among these surface proteins in its propensity to adhere to dextran/glucans. The complex crystal structure of GbpC with dextrose (β-d-glucose; Protein Data Bank ligand BGC) highlights exclusive structural features that facilitate this interaction with dextran. Targeted deletion mutant studies on GbpC's divergent loop region in the vicinity of a highly conserved calcium binding site confirm its role in biofilm formation. Finally, we present a model for adherence to dextran. The structure of GbpC highlights how artfully microbes have engineered the lectin-like folds to broaden their functional adherence repertoire.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>29685986</pmid><doi>10.1128/IAI.00146-18</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Bacterial Adhesion Biofilms Calcium-Binding Proteins Carrier Proteins - chemistry Carrier Proteins - physiology Crystallography Dextrans - chemistry DNA-Binding Proteins Lectins - chemistry Lectins - physiology Molecular Pathogenesis Receptors, Cell Surface - chemistry Receptors, Scavenger - chemistry Streptococcus mutans - physiology Sucrose - pharmacology Tumor Suppressor Proteins |
| title | Glucan Binding Protein C of Streptococcus mutans Mediates both Sucrose-Independent and Sucrose-Dependent Adherence |
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