Group A Streptococcal M1 Protein Provides Resistance against the Antimicrobial Activity of Histones
Histones are essential elements of chromatin structure and gene regulation in eukaryotes. An unexpected attribute of these nuclear proteins is their antimicrobial activity. A framework for histone release and function in host defense in vivo was revealed with the discovery of neutrophil extracellula...
Gespeichert in:
| Veröffentlicht in: | Scientific reports 2017-02, Vol.7 (1), p.43039-43039, Article 43039 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 43039 |
|---|---|
| container_issue | 1 |
| container_start_page | 43039 |
| container_title | Scientific reports |
| container_volume | 7 |
| creator | Döhrmann, Simon LaRock, Christopher N. Anderson, Ericka L. Cole, Jason N. Ryali, Brinda Stewart, Chelsea Nonejuie, Poochit Pogliano, Joe Corriden, Ross Ghosh, Partho Nizet, Victor |
| description | Histones are essential elements of chromatin structure and gene regulation in eukaryotes. An unexpected attribute of these nuclear proteins is their antimicrobial activity. A framework for histone release and function in host defense
in vivo
was revealed with the discovery of neutrophil extracellular traps, a specialized cell death process in which DNA-based structures containing histones are extruded to ensnare and kill bacteria. Investigating the susceptibility of various Gram-positive pathogens to histones, we found high-level resistance by one leading human pathogen, group A
Streptococcus
(GAS). A screen of isogenic mutants revealed that the highly surface-expressed M1 protein, a classical GAS virulence factor, was required for high-level histone resistance. Biochemical and microscopic analyses revealed that the N-terminal domain of M1 protein binds and inactivates histones before they reach their cell wall target of action. This finding illustrates a new pathogenic function for this classic GAS virulence factor, and highlights a potential innate immune evasion strategy that may be employed by other bacterial pathogens. |
| doi_str_mv | 10.1038/srep43039 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5318940</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1870645784</sourcerecordid><originalsourceid>FETCH-LOGICAL-c504t-237a5ab977b76bfcad24c3000545f70676d3e3376f7a003bd384753de7f505473</originalsourceid><addsrcrecordid>eNplkUtLAzEUhYMoKtWFf0ACblSo5jmZ2QhFfIGi-FiHTCZTI9OkJpmC_96U1lI1mxu43z05uQeAA4zOMKLleQxmyiii1QbYJYjxIaGEbK7dd8B-jB8oH04qhqttsENKQlBZVbtA3wTfT-EIvqSsk7z2WqsOPmD4FHwy1s3rzDYmwmcTbUzKaQPVWFkXE0zvBo5cshOrg69tHhzpZGc2fUHfwtuMe2fiHthqVRfN_rIOwNv11evl7fD-8ebucnQ_1ByxlL0KxVVdCVGLom61agjTdG6b8VagQhQNNZSKohUKIVo3tGSC08aIlmdG0AG4WOhO-3piGm1cCqqT02AnKnxJr6z83XH2XY79THKKy4qhLHC8FAj-szcxyYmN2nSdcsb3UeIy22BclCyjR3_QD98Hl78ncYWwIIzSIlMnCyqvJ-ag2pUZjOQ8PblKL7OH6-5X5E9WGThdADG33NiEtSf_qX0Duiqjvg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1901724336</pqid></control><display><type>article</type><title>Group A Streptococcal M1 Protein Provides Resistance against the Antimicrobial Activity of Histones</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Springer Nature OA Free Journals</source><source>Nature Free</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Döhrmann, Simon ; LaRock, Christopher N. ; Anderson, Ericka L. ; Cole, Jason N. ; Ryali, Brinda ; Stewart, Chelsea ; Nonejuie, Poochit ; Pogliano, Joe ; Corriden, Ross ; Ghosh, Partho ; Nizet, Victor</creator><creatorcontrib>Döhrmann, Simon ; LaRock, Christopher N. ; Anderson, Ericka L. ; Cole, Jason N. ; Ryali, Brinda ; Stewart, Chelsea ; Nonejuie, Poochit ; Pogliano, Joe ; Corriden, Ross ; Ghosh, Partho ; Nizet, Victor</creatorcontrib><description>Histones are essential elements of chromatin structure and gene regulation in eukaryotes. An unexpected attribute of these nuclear proteins is their antimicrobial activity. A framework for histone release and function in host defense
in vivo
was revealed with the discovery of neutrophil extracellular traps, a specialized cell death process in which DNA-based structures containing histones are extruded to ensnare and kill bacteria. Investigating the susceptibility of various Gram-positive pathogens to histones, we found high-level resistance by one leading human pathogen, group A
Streptococcus
(GAS). A screen of isogenic mutants revealed that the highly surface-expressed M1 protein, a classical GAS virulence factor, was required for high-level histone resistance. Biochemical and microscopic analyses revealed that the N-terminal domain of M1 protein binds and inactivates histones before they reach their cell wall target of action. This finding illustrates a new pathogenic function for this classic GAS virulence factor, and highlights a potential innate immune evasion strategy that may be employed by other bacterial pathogens.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep43039</identifier><identifier>PMID: 28220899</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13 ; 13/1 ; 13/106 ; 13/51 ; 14 ; 14/28 ; 14/34 ; 14/63 ; 38 ; 45 ; 45/70 ; 631/250/262 ; 631/326/1320 ; 64 ; 82 ; Antigens, Bacterial - metabolism ; Antigens, Bacterial - physiology ; Antimicrobial activity ; Antimicrobial agents ; Bacterial Outer Membrane Proteins - metabolism ; Bacterial Outer Membrane Proteins - physiology ; Carrier Proteins - metabolism ; Carrier Proteins - physiology ; Cell death ; Cell walls ; Chromatin ; Deoxyribonucleic acid ; DNA ; Gene regulation ; Histones ; Histones - metabolism ; Humanities and Social Sciences ; Humans ; Immune Evasion ; multidisciplinary ; Neutrophils - immunology ; Neutrophils - metabolism ; Pathogens ; Proteins ; Science ; Streptococcal Infections - metabolism ; Streptococcal Infections - microbiology ; Streptococcus ; Streptococcus infections ; Streptococcus pyogenes - metabolism ; Streptococcus pyogenes - pathogenicity ; Streptococcus pyogenes - physiology ; Virulence factors ; Virulence Factors - metabolism ; Virulence Factors - physiology</subject><ispartof>Scientific reports, 2017-02, Vol.7 (1), p.43039-43039, Article 43039</ispartof><rights>The Author(s) 2017</rights><rights>Copyright Nature Publishing Group Feb 2017</rights><rights>Copyright © 2017, The Author(s) 2017 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-237a5ab977b76bfcad24c3000545f70676d3e3376f7a003bd384753de7f505473</citedby><cites>FETCH-LOGICAL-c504t-237a5ab977b76bfcad24c3000545f70676d3e3376f7a003bd384753de7f505473</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/PMC5318940/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5318940/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,41120,42189,51576,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28220899$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Döhrmann, Simon</creatorcontrib><creatorcontrib>LaRock, Christopher N.</creatorcontrib><creatorcontrib>Anderson, Ericka L.</creatorcontrib><creatorcontrib>Cole, Jason N.</creatorcontrib><creatorcontrib>Ryali, Brinda</creatorcontrib><creatorcontrib>Stewart, Chelsea</creatorcontrib><creatorcontrib>Nonejuie, Poochit</creatorcontrib><creatorcontrib>Pogliano, Joe</creatorcontrib><creatorcontrib>Corriden, Ross</creatorcontrib><creatorcontrib>Ghosh, Partho</creatorcontrib><creatorcontrib>Nizet, Victor</creatorcontrib><title>Group A Streptococcal M1 Protein Provides Resistance against the Antimicrobial Activity of Histones</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Histones are essential elements of chromatin structure and gene regulation in eukaryotes. An unexpected attribute of these nuclear proteins is their antimicrobial activity. A framework for histone release and function in host defense
in vivo
was revealed with the discovery of neutrophil extracellular traps, a specialized cell death process in which DNA-based structures containing histones are extruded to ensnare and kill bacteria. Investigating the susceptibility of various Gram-positive pathogens to histones, we found high-level resistance by one leading human pathogen, group A
Streptococcus
(GAS). A screen of isogenic mutants revealed that the highly surface-expressed M1 protein, a classical GAS virulence factor, was required for high-level histone resistance. Biochemical and microscopic analyses revealed that the N-terminal domain of M1 protein binds and inactivates histones before they reach their cell wall target of action. This finding illustrates a new pathogenic function for this classic GAS virulence factor, and highlights a potential innate immune evasion strategy that may be employed by other bacterial pathogens.</description><subject>13</subject><subject>13/1</subject><subject>13/106</subject><subject>13/51</subject><subject>14</subject><subject>14/28</subject><subject>14/34</subject><subject>14/63</subject><subject>38</subject><subject>45</subject><subject>45/70</subject><subject>631/250/262</subject><subject>631/326/1320</subject><subject>64</subject><subject>82</subject><subject>Antigens, Bacterial - metabolism</subject><subject>Antigens, Bacterial - physiology</subject><subject>Antimicrobial activity</subject><subject>Antimicrobial agents</subject><subject>Bacterial Outer Membrane Proteins - metabolism</subject><subject>Bacterial Outer Membrane Proteins - physiology</subject><subject>Carrier Proteins - metabolism</subject><subject>Carrier Proteins - physiology</subject><subject>Cell death</subject><subject>Cell walls</subject><subject>Chromatin</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Gene regulation</subject><subject>Histones</subject><subject>Histones - metabolism</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Immune Evasion</subject><subject>multidisciplinary</subject><subject>Neutrophils - immunology</subject><subject>Neutrophils - metabolism</subject><subject>Pathogens</subject><subject>Proteins</subject><subject>Science</subject><subject>Streptococcal Infections - metabolism</subject><subject>Streptococcal Infections - microbiology</subject><subject>Streptococcus</subject><subject>Streptococcus infections</subject><subject>Streptococcus pyogenes - metabolism</subject><subject>Streptococcus pyogenes - pathogenicity</subject><subject>Streptococcus pyogenes - physiology</subject><subject>Virulence factors</subject><subject>Virulence Factors - metabolism</subject><subject>Virulence Factors - physiology</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><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>eNplkUtLAzEUhYMoKtWFf0ACblSo5jmZ2QhFfIGi-FiHTCZTI9OkJpmC_96U1lI1mxu43z05uQeAA4zOMKLleQxmyiii1QbYJYjxIaGEbK7dd8B-jB8oH04qhqttsENKQlBZVbtA3wTfT-EIvqSsk7z2WqsOPmD4FHwy1s3rzDYmwmcTbUzKaQPVWFkXE0zvBo5cshOrg69tHhzpZGc2fUHfwtuMe2fiHthqVRfN_rIOwNv11evl7fD-8ebucnQ_1ByxlL0KxVVdCVGLom61agjTdG6b8VagQhQNNZSKohUKIVo3tGSC08aIlmdG0AG4WOhO-3piGm1cCqqT02AnKnxJr6z83XH2XY79THKKy4qhLHC8FAj-szcxyYmN2nSdcsb3UeIy22BclCyjR3_QD98Hl78ncYWwIIzSIlMnCyqvJ-ag2pUZjOQ8PblKL7OH6-5X5E9WGThdADG33NiEtSf_qX0Duiqjvg</recordid><startdate>20170221</startdate><enddate>20170221</enddate><creator>Döhrmann, Simon</creator><creator>LaRock, Christopher N.</creator><creator>Anderson, Ericka L.</creator><creator>Cole, Jason N.</creator><creator>Ryali, Brinda</creator><creator>Stewart, Chelsea</creator><creator>Nonejuie, Poochit</creator><creator>Pogliano, Joe</creator><creator>Corriden, Ross</creator><creator>Ghosh, Partho</creator><creator>Nizet, Victor</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20170221</creationdate><title>Group A Streptococcal M1 Protein Provides Resistance against the Antimicrobial Activity of Histones</title><author>Döhrmann, Simon ; LaRock, Christopher N. ; Anderson, Ericka L. ; Cole, Jason N. ; Ryali, Brinda ; Stewart, Chelsea ; Nonejuie, Poochit ; Pogliano, Joe ; Corriden, Ross ; Ghosh, Partho ; Nizet, Victor</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-237a5ab977b76bfcad24c3000545f70676d3e3376f7a003bd384753de7f505473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>13</topic><topic>13/1</topic><topic>13/106</topic><topic>13/51</topic><topic>14</topic><topic>14/28</topic><topic>14/34</topic><topic>14/63</topic><topic>38</topic><topic>45</topic><topic>45/70</topic><topic>631/250/262</topic><topic>631/326/1320</topic><topic>64</topic><topic>82</topic><topic>Antigens, Bacterial - metabolism</topic><topic>Antigens, Bacterial - physiology</topic><topic>Antimicrobial activity</topic><topic>Antimicrobial agents</topic><topic>Bacterial Outer Membrane Proteins - metabolism</topic><topic>Bacterial Outer Membrane Proteins - physiology</topic><topic>Carrier Proteins - metabolism</topic><topic>Carrier Proteins - physiology</topic><topic>Cell death</topic><topic>Cell walls</topic><topic>Chromatin</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Gene regulation</topic><topic>Histones</topic><topic>Histones - metabolism</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Immune Evasion</topic><topic>multidisciplinary</topic><topic>Neutrophils - immunology</topic><topic>Neutrophils - metabolism</topic><topic>Pathogens</topic><topic>Proteins</topic><topic>Science</topic><topic>Streptococcal Infections - metabolism</topic><topic>Streptococcal Infections - microbiology</topic><topic>Streptococcus</topic><topic>Streptococcus infections</topic><topic>Streptococcus pyogenes - metabolism</topic><topic>Streptococcus pyogenes - pathogenicity</topic><topic>Streptococcus pyogenes - physiology</topic><topic>Virulence factors</topic><topic>Virulence Factors - metabolism</topic><topic>Virulence Factors - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Döhrmann, Simon</creatorcontrib><creatorcontrib>LaRock, Christopher N.</creatorcontrib><creatorcontrib>Anderson, Ericka L.</creatorcontrib><creatorcontrib>Cole, Jason N.</creatorcontrib><creatorcontrib>Ryali, Brinda</creatorcontrib><creatorcontrib>Stewart, Chelsea</creatorcontrib><creatorcontrib>Nonejuie, Poochit</creatorcontrib><creatorcontrib>Pogliano, Joe</creatorcontrib><creatorcontrib>Corriden, Ross</creatorcontrib><creatorcontrib>Ghosh, Partho</creatorcontrib><creatorcontrib>Nizet, Victor</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Döhrmann, Simon</au><au>LaRock, Christopher N.</au><au>Anderson, Ericka L.</au><au>Cole, Jason N.</au><au>Ryali, Brinda</au><au>Stewart, Chelsea</au><au>Nonejuie, Poochit</au><au>Pogliano, Joe</au><au>Corriden, Ross</au><au>Ghosh, Partho</au><au>Nizet, Victor</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Group A Streptococcal M1 Protein Provides Resistance against the Antimicrobial Activity of Histones</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2017-02-21</date><risdate>2017</risdate><volume>7</volume><issue>1</issue><spage>43039</spage><epage>43039</epage><pages>43039-43039</pages><artnum>43039</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Histones are essential elements of chromatin structure and gene regulation in eukaryotes. An unexpected attribute of these nuclear proteins is their antimicrobial activity. A framework for histone release and function in host defense
in vivo
was revealed with the discovery of neutrophil extracellular traps, a specialized cell death process in which DNA-based structures containing histones are extruded to ensnare and kill bacteria. Investigating the susceptibility of various Gram-positive pathogens to histones, we found high-level resistance by one leading human pathogen, group A
Streptococcus
(GAS). A screen of isogenic mutants revealed that the highly surface-expressed M1 protein, a classical GAS virulence factor, was required for high-level histone resistance. Biochemical and microscopic analyses revealed that the N-terminal domain of M1 protein binds and inactivates histones before they reach their cell wall target of action. This finding illustrates a new pathogenic function for this classic GAS virulence factor, and highlights a potential innate immune evasion strategy that may be employed by other bacterial pathogens.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28220899</pmid><doi>10.1038/srep43039</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2045-2322 |
| ispartof | Scientific reports, 2017-02, Vol.7 (1), p.43039-43039, Article 43039 |
| issn | 2045-2322 2045-2322 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5318940 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Springer Nature OA Free Journals; Nature Free; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | 13 13/1 13/106 13/51 14 14/28 14/34 14/63 38 45 45/70 631/250/262 631/326/1320 64 82 Antigens, Bacterial - metabolism Antigens, Bacterial - physiology Antimicrobial activity Antimicrobial agents Bacterial Outer Membrane Proteins - metabolism Bacterial Outer Membrane Proteins - physiology Carrier Proteins - metabolism Carrier Proteins - physiology Cell death Cell walls Chromatin Deoxyribonucleic acid DNA Gene regulation Histones Histones - metabolism Humanities and Social Sciences Humans Immune Evasion multidisciplinary Neutrophils - immunology Neutrophils - metabolism Pathogens Proteins Science Streptococcal Infections - metabolism Streptococcal Infections - microbiology Streptococcus Streptococcus infections Streptococcus pyogenes - metabolism Streptococcus pyogenes - pathogenicity Streptococcus pyogenes - physiology Virulence factors Virulence Factors - metabolism Virulence Factors - physiology |
| title | Group A Streptococcal M1 Protein Provides Resistance against the Antimicrobial Activity of Histones |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T04%3A28%3A24IST&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=Group%20A%20Streptococcal%20M1%20Protein%20Provides%20Resistance%20against%20the%20Antimicrobial%20Activity%20of%20Histones&rft.jtitle=Scientific%20reports&rft.au=D%C3%B6hrmann,%20Simon&rft.date=2017-02-21&rft.volume=7&rft.issue=1&rft.spage=43039&rft.epage=43039&rft.pages=43039-43039&rft.artnum=43039&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/srep43039&rft_dat=%3Cproquest_pubme%3E1870645784%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1901724336&rft_id=info:pmid/28220899&rfr_iscdi=true |