Immunogenic properties of Streptococcus agalactiae FbsA fragments
Several species of Gram-positive bacteria can avidly bind soluble and surface-associated fibrinogen (Fng), a property that is considered important in the pathogenesis of human infections. To gain insights into the mechanism by which group B Streptococcus (GBS), a frequent neonatal pathogen, interact...
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creator | Papasergi, Salvatore Lanza Cariccio, Veronica Pietrocola, Giampiero Domina, Maria D'Aliberti, Deborah Trunfio, Maria Grazia Signorino, Giacomo Peppoloni, Samuele Biondo, Carmelo Mancuso, Giuseppe Midiri, Angelina Rindi, Simonetta Teti, Giuseppe Speziale, Pietro Felici, Franco Beninati, Concetta |
description | Several species of Gram-positive bacteria can avidly bind soluble and surface-associated fibrinogen (Fng), a property that is considered important in the pathogenesis of human infections. To gain insights into the mechanism by which group B Streptococcus (GBS), a frequent neonatal pathogen, interacts with Fng, we have screened two phage displayed genomic GBS libraries. All of the Fng-binding phage clones contained inserts encoding fragments of FbsA, a protein displaying multiple repeats. Since the functional role of this protein is only partially understood, representative fragments were recombinantly expressed and analyzed for Fng binding affinity and ability to induce immune protection against GBS infection. Maternal immunization with 6pGST, a fragment containing five repeats, significantly protected mouse pups against lethal GBS challenge and these protective effects could be recapitulated by administration of anti-6pGST serum from adult animals. Notably, a monoclonal antibody that was capable of neutralizing Fng binding by 6pGST, but not a non-neutralizing antibody, could significantly protect pups against lethal GBS challenge. These data suggest that FbsA-Fng interaction promotes GBS pathogenesis and that blocking such interaction is a viable strategy to prevent or treat GBS infections. |
doi_str_mv | 10.1371/journal.pone.0075266 |
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To gain insights into the mechanism by which group B Streptococcus (GBS), a frequent neonatal pathogen, interacts with Fng, we have screened two phage displayed genomic GBS libraries. All of the Fng-binding phage clones contained inserts encoding fragments of FbsA, a protein displaying multiple repeats. Since the functional role of this protein is only partially understood, representative fragments were recombinantly expressed and analyzed for Fng binding affinity and ability to induce immune protection against GBS infection. Maternal immunization with 6pGST, a fragment containing five repeats, significantly protected mouse pups against lethal GBS challenge and these protective effects could be recapitulated by administration of anti-6pGST serum from adult animals. Notably, a monoclonal antibody that was capable of neutralizing Fng binding by 6pGST, but not a non-neutralizing antibody, could significantly protect pups against lethal GBS challenge. These data suggest that FbsA-Fng interaction promotes GBS pathogenesis and that blocking such interaction is a viable strategy to prevent or treat GBS infections.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0075266</identifier><identifier>PMID: 24086487</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Analysis ; Animals ; Antibodies, Monoclonal - immunology ; Arthritis ; Bacteria ; Bacterial Proteins - immunology ; Bacterial Proteins - metabolism ; Binding ; Biochemistry ; Carrier Proteins - immunology ; Carrier Proteins - metabolism ; Cloning ; Endocarditis ; Fibrin ; Fibrinogen ; Fibrinogen - metabolism ; Fragmentation ; Fragments ; Genomes ; Gram-positive bacteria ; Health aspects ; Humans ; Immunization ; Immunization - methods ; Immunogenicity ; Infection ; Infections ; Inserts ; Laboratories ; Medical screening ; Medicine ; Mice ; Monoclonal antibodies ; Neonates ; Neutralization Tests ; Neutralizing ; Newborn babies ; Pathogenesis ; Pathogens ; Peptide Library ; Phages ; Protein Binding ; Proteins ; Sepsis ; Staphylococcus aureus ; Streptococcus agalactiae ; Streptococcus agalactiae - immunology ; Streptococcus infections ; Streptococcus pneumoniae ; Streptococcus pyogenes ; Time Factors ; Toxoplasma gondii</subject><ispartof>PloS one, 2013-09, Vol.8 (9), p.e75266-e75266</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Papasergi et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Papasergi et al 2013 Papasergi et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-e9f6164789cca90be06158541f1443b4d1d088a0016b230bd8d013bceec043f43</citedby><cites>FETCH-LOGICAL-c692t-e9f6164789cca90be06158541f1443b4d1d088a0016b230bd8d013bceec043f43</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/PMC3782484/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3782484/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24086487$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Manganelli, Riccardo</contributor><creatorcontrib>Papasergi, Salvatore</creatorcontrib><creatorcontrib>Lanza Cariccio, Veronica</creatorcontrib><creatorcontrib>Pietrocola, Giampiero</creatorcontrib><creatorcontrib>Domina, Maria</creatorcontrib><creatorcontrib>D'Aliberti, Deborah</creatorcontrib><creatorcontrib>Trunfio, Maria Grazia</creatorcontrib><creatorcontrib>Signorino, Giacomo</creatorcontrib><creatorcontrib>Peppoloni, Samuele</creatorcontrib><creatorcontrib>Biondo, Carmelo</creatorcontrib><creatorcontrib>Mancuso, Giuseppe</creatorcontrib><creatorcontrib>Midiri, Angelina</creatorcontrib><creatorcontrib>Rindi, Simonetta</creatorcontrib><creatorcontrib>Teti, Giuseppe</creatorcontrib><creatorcontrib>Speziale, Pietro</creatorcontrib><creatorcontrib>Felici, Franco</creatorcontrib><creatorcontrib>Beninati, Concetta</creatorcontrib><title>Immunogenic properties of Streptococcus agalactiae FbsA fragments</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Several species of Gram-positive bacteria can avidly bind soluble and surface-associated fibrinogen (Fng), a property that is considered important in the pathogenesis of human infections. To gain insights into the mechanism by which group B Streptococcus (GBS), a frequent neonatal pathogen, interacts with Fng, we have screened two phage displayed genomic GBS libraries. All of the Fng-binding phage clones contained inserts encoding fragments of FbsA, a protein displaying multiple repeats. Since the functional role of this protein is only partially understood, representative fragments were recombinantly expressed and analyzed for Fng binding affinity and ability to induce immune protection against GBS infection. Maternal immunization with 6pGST, a fragment containing five repeats, significantly protected mouse pups against lethal GBS challenge and these protective effects could be recapitulated by administration of anti-6pGST serum from adult animals. Notably, a monoclonal antibody that was capable of neutralizing Fng binding by 6pGST, but not a non-neutralizing antibody, could significantly protect pups against lethal GBS challenge. These data suggest that FbsA-Fng interaction promotes GBS pathogenesis and that blocking such interaction is a viable strategy to prevent or treat GBS infections.</description><subject>Analysis</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Arthritis</subject><subject>Bacteria</subject><subject>Bacterial Proteins - immunology</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding</subject><subject>Biochemistry</subject><subject>Carrier Proteins - immunology</subject><subject>Carrier Proteins - metabolism</subject><subject>Cloning</subject><subject>Endocarditis</subject><subject>Fibrin</subject><subject>Fibrinogen</subject><subject>Fibrinogen - metabolism</subject><subject>Fragmentation</subject><subject>Fragments</subject><subject>Genomes</subject><subject>Gram-positive bacteria</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Immunization</subject><subject>Immunization - methods</subject><subject>Immunogenicity</subject><subject>Infection</subject><subject>Infections</subject><subject>Inserts</subject><subject>Laboratories</subject><subject>Medical screening</subject><subject>Medicine</subject><subject>Mice</subject><subject>Monoclonal antibodies</subject><subject>Neonates</subject><subject>Neutralization Tests</subject><subject>Neutralizing</subject><subject>Newborn babies</subject><subject>Pathogenesis</subject><subject>Pathogens</subject><subject>Peptide Library</subject><subject>Phages</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Sepsis</subject><subject>Staphylococcus aureus</subject><subject>Streptococcus agalactiae</subject><subject>Streptococcus agalactiae - 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To gain insights into the mechanism by which group B Streptococcus (GBS), a frequent neonatal pathogen, interacts with Fng, we have screened two phage displayed genomic GBS libraries. All of the Fng-binding phage clones contained inserts encoding fragments of FbsA, a protein displaying multiple repeats. Since the functional role of this protein is only partially understood, representative fragments were recombinantly expressed and analyzed for Fng binding affinity and ability to induce immune protection against GBS infection. Maternal immunization with 6pGST, a fragment containing five repeats, significantly protected mouse pups against lethal GBS challenge and these protective effects could be recapitulated by administration of anti-6pGST serum from adult animals. Notably, a monoclonal antibody that was capable of neutralizing Fng binding by 6pGST, but not a non-neutralizing antibody, could significantly protect pups against lethal GBS challenge. These data suggest that FbsA-Fng interaction promotes GBS pathogenesis and that blocking such interaction is a viable strategy to prevent or treat GBS infections.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24086487</pmid><doi>10.1371/journal.pone.0075266</doi><tpages>e75266</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
subjects | Analysis Animals Antibodies, Monoclonal - immunology Arthritis Bacteria Bacterial Proteins - immunology Bacterial Proteins - metabolism Binding Biochemistry Carrier Proteins - immunology Carrier Proteins - metabolism Cloning Endocarditis Fibrin Fibrinogen Fibrinogen - metabolism Fragmentation Fragments Genomes Gram-positive bacteria Health aspects Humans Immunization Immunization - methods Immunogenicity Infection Infections Inserts Laboratories Medical screening Medicine Mice Monoclonal antibodies Neonates Neutralization Tests Neutralizing Newborn babies Pathogenesis Pathogens Peptide Library Phages Protein Binding Proteins Sepsis Staphylococcus aureus Streptococcus agalactiae Streptococcus agalactiae - immunology Streptococcus infections Streptococcus pneumoniae Streptococcus pyogenes Time Factors Toxoplasma gondii |
title | Immunogenic properties of Streptococcus agalactiae FbsA fragments |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T13%3A35%3A58IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Immunogenic%20properties%20of%20Streptococcus%20agalactiae%20FbsA%20fragments&rft.jtitle=PloS%20one&rft.au=Papasergi,%20Salvatore&rft.date=2013-09-24&rft.volume=8&rft.issue=9&rft.spage=e75266&rft.epage=e75266&rft.pages=e75266-e75266&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0075266&rft_dat=%3Cgale_plos_%3EA478820414%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1435972253&rft_id=info:pmid/24086487&rft_galeid=A478820414&rft_doaj_id=oai_doaj_org_article_2b48187e691647b2a9b5bd13745db27a&rfr_iscdi=true |