Loading…
Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation
Binding of the host complement regulator, factor H (FH), by some pathogenic microbes constitutes an important virulence mechanism, whereby complement is broken down to help microbes survive in the host. Although it has been hypothesized for the past two decades that GBS type III binds FH via sialic...
Saved in:
Published in: | The FASEB journal 2009-11, Vol.23 (11), p.3967-3977 |
---|---|
Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c4509-3b6745073501be9430ae458b5342ccfc8d2c41831e89efe3ccf7e8ef5a9c91fa3 |
---|---|
cites | cdi_FETCH-LOGICAL-c4509-3b6745073501be9430ae458b5342ccfc8d2c41831e89efe3ccf7e8ef5a9c91fa3 |
container_end_page | 3977 |
container_issue | 11 |
container_start_page | 3967 |
container_title | The FASEB journal |
container_volume | 23 |
creator | Maruvada, Ravi Prasadarao, Nemani V Rubens, C.E |
description | Binding of the host complement regulator, factor H (FH), by some pathogenic microbes constitutes an important virulence mechanism, whereby complement is broken down to help microbes survive in the host. Although it has been hypothesized for the past two decades that GBS type III binds FH via sialic acid present on its capsule, neither the binding of FH to GBS has been demonstrated nor the mechanism of interaction identified. We observed that FH bound to both wild-type and capsule or sialic acid-deficient GBS that were used as negative controls. Wild-type and acapsular GBS were incubated with serum or pure FH degraded almost 90% of C3b, suggesting that the GBS-bound FH maintained cofactor activity. In addition, dot-blot analysis showed ~5-10% of C5 and C9 formation, as compared to an Escherichia coli control, suggesting breakdown at the C3b level. Protease treatment of the bacteria completely abolished binding of FH. Using overlay assays and mass spectroscopic analysis, we identified the FH receptor as the streptococcal histidine triad (SHT) surface protein. The ability of binding FH to SHT was further confirmed by using recombinant SHT. This report describes the identification of the SHT as an FH-binding protein on the surface of GBS type III, revealing a novel mechanism by which the bacterium acquires FH to evade complement opsonization.--Maruvada, R., Prasadarao, N. V., Rubens, C. E. Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation. |
doi_str_mv | 10.1096/fj.09-138149 |
format | article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2775014</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>734114778</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4509-3b6745073501be9430ae458b5342ccfc8d2c41831e89efe3ccf7e8ef5a9c91fa3</originalsourceid><addsrcrecordid>eNp9krFv3CAUh1GVqrkm3TK3bFnqFAzGsFRKol7TKlKGa2aEuceFq20csBPdf19OPqXtkgn0-PjeQz8QOqPkghIlvrjtBVEFZZJy9QYtaMVIIaQgR2hBpCoLIZg8Ru9T2hJCKKHiHTqmShApymqBfl_ax8knP_rQ4-CwM3YMEd_gZocN7sMTtDhNMZcBDzGM4DPW400M04Cv8GqMMIzBBmuntAe6jCRsQze00EE_4jVsolmbvf8UvXWmTfDhsJ6g--W3X9c3xe3d9x_Xl7eF5VV-CmtEnTc1qwhtQHFGDPBKNhXjpbXOynVpOZWMglTggOVaDRJcZZRV1Bl2gr7O3mFqOljbPEY0rR6i70zc6WC8_v-k9w96E550Wde5J8-C84MghscJ0qg7nyy0rekhTEnXjFPK61pm8vNM2hhSiuBeulCi9_Fot9VE6TmejH_8d7K_8CGPDMgZePYt7F6V6eXqqlz-JOrF_Wm-6kzQZhN90verklCWI1f5I0j2B-xPp-s</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>734114778</pqid></control><display><type>article</type><title>Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation</title><source>Wiley</source><creator>Maruvada, Ravi ; Prasadarao, Nemani V ; Rubens, C.E</creator><creatorcontrib>Maruvada, Ravi ; Prasadarao, Nemani V ; Rubens, C.E</creatorcontrib><description>Binding of the host complement regulator, factor H (FH), by some pathogenic microbes constitutes an important virulence mechanism, whereby complement is broken down to help microbes survive in the host. Although it has been hypothesized for the past two decades that GBS type III binds FH via sialic acid present on its capsule, neither the binding of FH to GBS has been demonstrated nor the mechanism of interaction identified. We observed that FH bound to both wild-type and capsule or sialic acid-deficient GBS that were used as negative controls. Wild-type and acapsular GBS were incubated with serum or pure FH degraded almost 90% of C3b, suggesting that the GBS-bound FH maintained cofactor activity. In addition, dot-blot analysis showed ~5-10% of C5 and C9 formation, as compared to an Escherichia coli control, suggesting breakdown at the C3b level. Protease treatment of the bacteria completely abolished binding of FH. Using overlay assays and mass spectroscopic analysis, we identified the FH receptor as the streptococcal histidine triad (SHT) surface protein. The ability of binding FH to SHT was further confirmed by using recombinant SHT. This report describes the identification of the SHT as an FH-binding protein on the surface of GBS type III, revealing a novel mechanism by which the bacterium acquires FH to evade complement opsonization.--Maruvada, R., Prasadarao, N. V., Rubens, C. E. Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation.</description><identifier>ISSN: 0892-6638</identifier><identifier>EISSN: 1530-6860</identifier><identifier>DOI: 10.1096/fj.09-138149</identifier><identifier>PMID: 19608625</identifier><language>eng</language><publisher>United States: The Federation of American Societies for Experimental Biology</publisher><subject>Carrier Proteins - metabolism ; Complement C3b - immunology ; Complement C3b - metabolism ; Complement Factor H - immunology ; Complement Factor H - metabolism ; CRASP ; Humans ; LC-MS ; membrane attack complex ; pathogenecity islands ; protease treatment ; Research Communications ; streptococcal histidine triad protein ; Streptococcus agalactiae - immunology ; Streptococcus agalactiae - metabolism</subject><ispartof>The FASEB journal, 2009-11, Vol.23 (11), p.3967-3977</ispartof><rights>FASEB</rights><rights>2009 FASEB 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4509-3b6745073501be9430ae458b5342ccfc8d2c41831e89efe3ccf7e8ef5a9c91fa3</citedby><cites>FETCH-LOGICAL-c4509-3b6745073501be9430ae458b5342ccfc8d2c41831e89efe3ccf7e8ef5a9c91fa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19608625$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Maruvada, Ravi</creatorcontrib><creatorcontrib>Prasadarao, Nemani V</creatorcontrib><creatorcontrib>Rubens, C.E</creatorcontrib><title>Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation</title><title>The FASEB journal</title><addtitle>FASEB J</addtitle><description>Binding of the host complement regulator, factor H (FH), by some pathogenic microbes constitutes an important virulence mechanism, whereby complement is broken down to help microbes survive in the host. Although it has been hypothesized for the past two decades that GBS type III binds FH via sialic acid present on its capsule, neither the binding of FH to GBS has been demonstrated nor the mechanism of interaction identified. We observed that FH bound to both wild-type and capsule or sialic acid-deficient GBS that were used as negative controls. Wild-type and acapsular GBS were incubated with serum or pure FH degraded almost 90% of C3b, suggesting that the GBS-bound FH maintained cofactor activity. In addition, dot-blot analysis showed ~5-10% of C5 and C9 formation, as compared to an Escherichia coli control, suggesting breakdown at the C3b level. Protease treatment of the bacteria completely abolished binding of FH. Using overlay assays and mass spectroscopic analysis, we identified the FH receptor as the streptococcal histidine triad (SHT) surface protein. The ability of binding FH to SHT was further confirmed by using recombinant SHT. This report describes the identification of the SHT as an FH-binding protein on the surface of GBS type III, revealing a novel mechanism by which the bacterium acquires FH to evade complement opsonization.--Maruvada, R., Prasadarao, N. V., Rubens, C. E. Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation.</description><subject>Carrier Proteins - metabolism</subject><subject>Complement C3b - immunology</subject><subject>Complement C3b - metabolism</subject><subject>Complement Factor H - immunology</subject><subject>Complement Factor H - metabolism</subject><subject>CRASP</subject><subject>Humans</subject><subject>LC-MS</subject><subject>membrane attack complex</subject><subject>pathogenecity islands</subject><subject>protease treatment</subject><subject>Research Communications</subject><subject>streptococcal histidine triad protein</subject><subject>Streptococcus agalactiae - immunology</subject><subject>Streptococcus agalactiae - metabolism</subject><issn>0892-6638</issn><issn>1530-6860</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNp9krFv3CAUh1GVqrkm3TK3bFnqFAzGsFRKol7TKlKGa2aEuceFq20csBPdf19OPqXtkgn0-PjeQz8QOqPkghIlvrjtBVEFZZJy9QYtaMVIIaQgR2hBpCoLIZg8Ru9T2hJCKKHiHTqmShApymqBfl_ax8knP_rQ4-CwM3YMEd_gZocN7sMTtDhNMZcBDzGM4DPW400M04Cv8GqMMIzBBmuntAe6jCRsQze00EE_4jVsolmbvf8UvXWmTfDhsJ6g--W3X9c3xe3d9x_Xl7eF5VV-CmtEnTc1qwhtQHFGDPBKNhXjpbXOynVpOZWMglTggOVaDRJcZZRV1Bl2gr7O3mFqOljbPEY0rR6i70zc6WC8_v-k9w96E550Wde5J8-C84MghscJ0qg7nyy0rekhTEnXjFPK61pm8vNM2hhSiuBeulCi9_Fot9VE6TmejH_8d7K_8CGPDMgZePYt7F6V6eXqqlz-JOrF_Wm-6kzQZhN90verklCWI1f5I0j2B-xPp-s</recordid><startdate>200911</startdate><enddate>200911</enddate><creator>Maruvada, Ravi</creator><creator>Prasadarao, Nemani V</creator><creator>Rubens, C.E</creator><general>The Federation of American Societies for Experimental Biology</general><scope>FBQ</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>5PM</scope></search><sort><creationdate>200911</creationdate><title>Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation</title><author>Maruvada, Ravi ; Prasadarao, Nemani V ; Rubens, C.E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4509-3b6745073501be9430ae458b5342ccfc8d2c41831e89efe3ccf7e8ef5a9c91fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Carrier Proteins - metabolism</topic><topic>Complement C3b - immunology</topic><topic>Complement C3b - metabolism</topic><topic>Complement Factor H - immunology</topic><topic>Complement Factor H - metabolism</topic><topic>CRASP</topic><topic>Humans</topic><topic>LC-MS</topic><topic>membrane attack complex</topic><topic>pathogenecity islands</topic><topic>protease treatment</topic><topic>Research Communications</topic><topic>streptococcal histidine triad protein</topic><topic>Streptococcus agalactiae - immunology</topic><topic>Streptococcus agalactiae - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Maruvada, Ravi</creatorcontrib><creatorcontrib>Prasadarao, Nemani V</creatorcontrib><creatorcontrib>Rubens, C.E</creatorcontrib><collection>AGRIS</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>PubMed Central (Full Participant titles)</collection><jtitle>The FASEB journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Maruvada, Ravi</au><au>Prasadarao, Nemani V</au><au>Rubens, C.E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation</atitle><jtitle>The FASEB journal</jtitle><addtitle>FASEB J</addtitle><date>2009-11</date><risdate>2009</risdate><volume>23</volume><issue>11</issue><spage>3967</spage><epage>3977</epage><pages>3967-3977</pages><issn>0892-6638</issn><eissn>1530-6860</eissn><abstract>Binding of the host complement regulator, factor H (FH), by some pathogenic microbes constitutes an important virulence mechanism, whereby complement is broken down to help microbes survive in the host. Although it has been hypothesized for the past two decades that GBS type III binds FH via sialic acid present on its capsule, neither the binding of FH to GBS has been demonstrated nor the mechanism of interaction identified. We observed that FH bound to both wild-type and capsule or sialic acid-deficient GBS that were used as negative controls. Wild-type and acapsular GBS were incubated with serum or pure FH degraded almost 90% of C3b, suggesting that the GBS-bound FH maintained cofactor activity. In addition, dot-blot analysis showed ~5-10% of C5 and C9 formation, as compared to an Escherichia coli control, suggesting breakdown at the C3b level. Protease treatment of the bacteria completely abolished binding of FH. Using overlay assays and mass spectroscopic analysis, we identified the FH receptor as the streptococcal histidine triad (SHT) surface protein. The ability of binding FH to SHT was further confirmed by using recombinant SHT. This report describes the identification of the SHT as an FH-binding protein on the surface of GBS type III, revealing a novel mechanism by which the bacterium acquires FH to evade complement opsonization.--Maruvada, R., Prasadarao, N. V., Rubens, C. E. Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation.</abstract><cop>United States</cop><pub>The Federation of American Societies for Experimental Biology</pub><pmid>19608625</pmid><doi>10.1096/fj.09-138149</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0892-6638 |
ispartof | The FASEB journal, 2009-11, Vol.23 (11), p.3967-3977 |
issn | 0892-6638 1530-6860 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2775014 |
source | Wiley |
subjects | Carrier Proteins - metabolism Complement C3b - immunology Complement C3b - metabolism Complement Factor H - immunology Complement Factor H - metabolism CRASP Humans LC-MS membrane attack complex pathogenecity islands protease treatment Research Communications streptococcal histidine triad protein Streptococcus agalactiae - immunology Streptococcus agalactiae - metabolism |
title | Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T22%3A27%3A33IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Acquisition%20of%20factor%20H%20by%20a%20novel%20surface%20protein%20on%20group%20B%20Streptococcus%20promotes%20complement%20degradation&rft.jtitle=The%20FASEB%20journal&rft.au=Maruvada,%20Ravi&rft.date=2009-11&rft.volume=23&rft.issue=11&rft.spage=3967&rft.epage=3977&rft.pages=3967-3977&rft.issn=0892-6638&rft.eissn=1530-6860&rft_id=info:doi/10.1096/fj.09-138149&rft_dat=%3Cproquest_pubme%3E734114778%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c4509-3b6745073501be9430ae458b5342ccfc8d2c41831e89efe3ccf7e8ef5a9c91fa3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=734114778&rft_id=info:pmid/19608625&rfr_iscdi=true |