A peptide factor secreted by Staphylococcus pseudintermedius exhibits properties of both bacteriocins and virulence factors
Staphylococcus pseudintermedius is a common commensal bacterium colonizing the skin and mucosal surfaces of household animals. However, it has recently emerged as a dangerous opportunistic pathogen, comparable to S. aureus for humans. The epidemiological situation is further complicated by the incre...
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creator | Wladyka, Benedykt Piejko, Marcin Bzowska, Monika Pieta, Piotr Krzysik, Monika Mazurek, Łukasz Guevara-Lora, Ibeth Bukowski, Michał Sabat, Artur J. Friedrich, Alexander W. Bonar, Emilia Międzobrodzki, Jacek Dubin, Adam Mak, Paweł |
description | Staphylococcus pseudintermedius
is a common commensal bacterium colonizing the skin and mucosal surfaces of household animals. However, it has recently emerged as a dangerous opportunistic pathogen, comparable to
S. aureus
for humans. The epidemiological situation is further complicated by the increasing number of methicillin-resistant
S. pseudintermedius
infections and evidence of gene transmission driving antibiotic resistance between staphylococci colonizing human and zoonotic hosts. In the present study, we describe a unique peptide, BacSp222, that possesses features characteristic of both bacteriocins and virulence factors. BacSp222 is secreted in high quantities by
S. pseudintermedius
strain 222 isolated from dog skin lesions. This linear, fifty-amino-acid highly cationic peptide is plasmid-encoded and does not exhibit significant sequence similarities to any other known peptides or proteins. BacSp222 kills gram-positive bacteria (at doses ranging from 0.1 to several micromol/l) but also demonstrates significant cytotoxic activities towards eukaryotic cells at slightly higher concentrations. Moreover, at nanomolar concentrations, the peptide also possesses modulatory properties, efficiently enhancing interferon gamma-induced nitric oxide release in murine macrophage-like cell lines. BacSp222 appears to be one of the first examples of multifunctional peptides that breaks the convention of splitting bacteriocins and virulence factors into two unrelated groups. |
doi_str_mv | 10.1038/srep14569 |
format | Article |
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is a common commensal bacterium colonizing the skin and mucosal surfaces of household animals. However, it has recently emerged as a dangerous opportunistic pathogen, comparable to
S. aureus
for humans. The epidemiological situation is further complicated by the increasing number of methicillin-resistant
S. pseudintermedius
infections and evidence of gene transmission driving antibiotic resistance between staphylococci colonizing human and zoonotic hosts. In the present study, we describe a unique peptide, BacSp222, that possesses features characteristic of both bacteriocins and virulence factors. BacSp222 is secreted in high quantities by
S. pseudintermedius
strain 222 isolated from dog skin lesions. This linear, fifty-amino-acid highly cationic peptide is plasmid-encoded and does not exhibit significant sequence similarities to any other known peptides or proteins. BacSp222 kills gram-positive bacteria (at doses ranging from 0.1 to several micromol/l) but also demonstrates significant cytotoxic activities towards eukaryotic cells at slightly higher concentrations. Moreover, at nanomolar concentrations, the peptide also possesses modulatory properties, efficiently enhancing interferon gamma-induced nitric oxide release in murine macrophage-like cell lines. BacSp222 appears to be one of the first examples of multifunctional peptides that breaks the convention of splitting bacteriocins and virulence factors into two unrelated groups.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep14569</identifier><identifier>PMID: 26411997</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13 ; 13/106 ; 14 ; 14/34 ; 14/63 ; 38/22 ; 38/23 ; 38/77 ; 631/1647/2230/2233 ; 631/250/255 ; 631/326/421 ; 631/45/611 ; 64 ; 82/16 ; 82/58 ; 82/81 ; Amino Acid Sequence ; Animals ; Antibiotic resistance ; Bacteria ; Bacteriocins ; Bacteriocins - chemistry ; Bacteriocins - isolation & purification ; Bacteriocins - pharmacology ; Base Sequence ; Cell Line ; Cell lines ; Cell Survival - drug effects ; Cytotoxicity ; Drug resistance ; Gram-positive bacteria ; Gram-Positive Bacteria - drug effects ; Humanities and Social Sciences ; Humans ; Macrophages ; Methicillin ; Microbial Sensitivity Tests ; Molecular Sequence Data ; Mucosa ; multidisciplinary ; Nitric oxide ; Nitric Oxide - biosynthesis ; Nitric Oxide Synthase Type II - metabolism ; Opportunist infection ; Peptides ; Peptides - chemistry ; Peptides - isolation & purification ; Peptides - pharmacology ; Protein Stability ; Science ; Sequence Alignment ; Skin diseases ; Splitting ; Staphylococcus - genetics ; Staphylococcus - metabolism ; Staphylococcus - pathogenicity ; Staphylococcus aureus ; Virulence factors ; Virulence Factors - chemistry ; Virulence Factors - isolation & purification ; Virulence Factors - pharmacology</subject><ispartof>Scientific reports, 2015-09, Vol.5 (1), p.14569-14569, Article 14569</ispartof><rights>The Author(s) 2015</rights><rights>Copyright Nature Publishing Group Sep 2015</rights><rights>Copyright © 2015, Macmillan Publishers Limited 2015 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-3b35db68adb29ba08c14af57b7d2fc0c7bca1a8c541d1ae21da6772e44ac22553</citedby><cites>FETCH-LOGICAL-c438t-3b35db68adb29ba08c14af57b7d2fc0c7bca1a8c541d1ae21da6772e44ac22553</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/PMC4585962/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4585962/$$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/26411997$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wladyka, Benedykt</creatorcontrib><creatorcontrib>Piejko, Marcin</creatorcontrib><creatorcontrib>Bzowska, Monika</creatorcontrib><creatorcontrib>Pieta, Piotr</creatorcontrib><creatorcontrib>Krzysik, Monika</creatorcontrib><creatorcontrib>Mazurek, Łukasz</creatorcontrib><creatorcontrib>Guevara-Lora, Ibeth</creatorcontrib><creatorcontrib>Bukowski, Michał</creatorcontrib><creatorcontrib>Sabat, Artur J.</creatorcontrib><creatorcontrib>Friedrich, Alexander W.</creatorcontrib><creatorcontrib>Bonar, Emilia</creatorcontrib><creatorcontrib>Międzobrodzki, Jacek</creatorcontrib><creatorcontrib>Dubin, Adam</creatorcontrib><creatorcontrib>Mak, Paweł</creatorcontrib><title>A peptide factor secreted by Staphylococcus pseudintermedius exhibits properties of both bacteriocins and virulence factors</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Staphylococcus pseudintermedius
is a common commensal bacterium colonizing the skin and mucosal surfaces of household animals. However, it has recently emerged as a dangerous opportunistic pathogen, comparable to
S. aureus
for humans. The epidemiological situation is further complicated by the increasing number of methicillin-resistant
S. pseudintermedius
infections and evidence of gene transmission driving antibiotic resistance between staphylococci colonizing human and zoonotic hosts. In the present study, we describe a unique peptide, BacSp222, that possesses features characteristic of both bacteriocins and virulence factors. BacSp222 is secreted in high quantities by
S. pseudintermedius
strain 222 isolated from dog skin lesions. This linear, fifty-amino-acid highly cationic peptide is plasmid-encoded and does not exhibit significant sequence similarities to any other known peptides or proteins. BacSp222 kills gram-positive bacteria (at doses ranging from 0.1 to several micromol/l) but also demonstrates significant cytotoxic activities towards eukaryotic cells at slightly higher concentrations. Moreover, at nanomolar concentrations, the peptide also possesses modulatory properties, efficiently enhancing interferon gamma-induced nitric oxide release in murine macrophage-like cell lines. BacSp222 appears to be one of the first examples of multifunctional peptides that breaks the convention of splitting bacteriocins and virulence factors into two unrelated groups.</description><subject>13</subject><subject>13/106</subject><subject>14</subject><subject>14/34</subject><subject>14/63</subject><subject>38/22</subject><subject>38/23</subject><subject>38/77</subject><subject>631/1647/2230/2233</subject><subject>631/250/255</subject><subject>631/326/421</subject><subject>631/45/611</subject><subject>64</subject><subject>82/16</subject><subject>82/58</subject><subject>82/81</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibiotic resistance</subject><subject>Bacteria</subject><subject>Bacteriocins</subject><subject>Bacteriocins - chemistry</subject><subject>Bacteriocins - isolation & purification</subject><subject>Bacteriocins - pharmacology</subject><subject>Base Sequence</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Cell Survival - drug effects</subject><subject>Cytotoxicity</subject><subject>Drug resistance</subject><subject>Gram-positive bacteria</subject><subject>Gram-Positive Bacteria - drug effects</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Macrophages</subject><subject>Methicillin</subject><subject>Microbial Sensitivity Tests</subject><subject>Molecular Sequence Data</subject><subject>Mucosa</subject><subject>multidisciplinary</subject><subject>Nitric oxide</subject><subject>Nitric Oxide - biosynthesis</subject><subject>Nitric Oxide Synthase Type II - metabolism</subject><subject>Opportunist infection</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - isolation & purification</subject><subject>Peptides - pharmacology</subject><subject>Protein Stability</subject><subject>Science</subject><subject>Sequence Alignment</subject><subject>Skin diseases</subject><subject>Splitting</subject><subject>Staphylococcus - genetics</subject><subject>Staphylococcus - metabolism</subject><subject>Staphylococcus - pathogenicity</subject><subject>Staphylococcus aureus</subject><subject>Virulence factors</subject><subject>Virulence Factors - chemistry</subject><subject>Virulence Factors - isolation & purification</subject><subject>Virulence Factors - pharmacology</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</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>eNplkV1rFDEYhYMottRe-Ack4I0Kq_mcydwIpVgVCr2oXod8vNNNmU3GJFO6-OdN2XZZNTcJOQ_nPclB6DUlHynh6lPJMFMhu-EZOmZEyBXjjD0_OB-h01JuSVuSDYIOL9ER6wSlw9Afo99neIa5Bg94NK6mjAu4DBU8tlt8Xc283k7JJeeWgucCiw-xQt6AD-0C7tfBhtqUnGbINUDBacQ21TW2zQ5ySC7Egk30-C7kZYLoniaVV-jFaKYCp4_7Cfp58eXH-bfV5dXX7-dnlysnuKorbrn0tlPGWzZYQ5Sjwoyyt71noyOut85Qo5wU1FMDjHrT9T0DIYxjTEp-gj7vfOfFtuAOYs1m0nMOG5O3Opmg_1ZiWOubdKeFVHLoWDN492iQ068FStWbUBxMk4mQlqJpTxXpuSK8oW__QW_TkmN7nqaq_XgnFSeNer-jXE6lFTjuw1CiH1rV-1Yb--Yw_Z586rABH3ZAaVK8gXww8j-3P83EsB4</recordid><startdate>20150928</startdate><enddate>20150928</enddate><creator>Wladyka, Benedykt</creator><creator>Piejko, Marcin</creator><creator>Bzowska, Monika</creator><creator>Pieta, Piotr</creator><creator>Krzysik, Monika</creator><creator>Mazurek, Łukasz</creator><creator>Guevara-Lora, Ibeth</creator><creator>Bukowski, Michał</creator><creator>Sabat, Artur J.</creator><creator>Friedrich, Alexander W.</creator><creator>Bonar, Emilia</creator><creator>Międzobrodzki, Jacek</creator><creator>Dubin, Adam</creator><creator>Mak, Paweł</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>20150928</creationdate><title>A peptide factor secreted by Staphylococcus pseudintermedius exhibits properties of both bacteriocins and virulence factors</title><author>Wladyka, Benedykt ; Piejko, Marcin ; Bzowska, Monika ; Pieta, Piotr ; Krzysik, Monika ; Mazurek, Łukasz ; Guevara-Lora, Ibeth ; Bukowski, Michał ; Sabat, Artur J. ; Friedrich, Alexander W. ; Bonar, Emilia ; Międzobrodzki, Jacek ; Dubin, Adam ; Mak, Paweł</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-3b35db68adb29ba08c14af57b7d2fc0c7bca1a8c541d1ae21da6772e44ac22553</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>13</topic><topic>13/106</topic><topic>14</topic><topic>14/34</topic><topic>14/63</topic><topic>38/22</topic><topic>38/23</topic><topic>38/77</topic><topic>631/1647/2230/2233</topic><topic>631/250/255</topic><topic>631/326/421</topic><topic>631/45/611</topic><topic>64</topic><topic>82/16</topic><topic>82/58</topic><topic>82/81</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibiotic resistance</topic><topic>Bacteria</topic><topic>Bacteriocins</topic><topic>Bacteriocins - chemistry</topic><topic>Bacteriocins - isolation & purification</topic><topic>Bacteriocins - pharmacology</topic><topic>Base Sequence</topic><topic>Cell Line</topic><topic>Cell lines</topic><topic>Cell Survival - drug effects</topic><topic>Cytotoxicity</topic><topic>Drug resistance</topic><topic>Gram-positive bacteria</topic><topic>Gram-Positive Bacteria - drug effects</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Macrophages</topic><topic>Methicillin</topic><topic>Microbial Sensitivity Tests</topic><topic>Molecular Sequence Data</topic><topic>Mucosa</topic><topic>multidisciplinary</topic><topic>Nitric oxide</topic><topic>Nitric Oxide - biosynthesis</topic><topic>Nitric Oxide Synthase Type II - metabolism</topic><topic>Opportunist infection</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - isolation & purification</topic><topic>Peptides - pharmacology</topic><topic>Protein Stability</topic><topic>Science</topic><topic>Sequence Alignment</topic><topic>Skin diseases</topic><topic>Splitting</topic><topic>Staphylococcus - genetics</topic><topic>Staphylococcus - metabolism</topic><topic>Staphylococcus - pathogenicity</topic><topic>Staphylococcus aureus</topic><topic>Virulence factors</topic><topic>Virulence Factors - chemistry</topic><topic>Virulence Factors - isolation & purification</topic><topic>Virulence Factors - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wladyka, Benedykt</creatorcontrib><creatorcontrib>Piejko, Marcin</creatorcontrib><creatorcontrib>Bzowska, Monika</creatorcontrib><creatorcontrib>Pieta, Piotr</creatorcontrib><creatorcontrib>Krzysik, Monika</creatorcontrib><creatorcontrib>Mazurek, Łukasz</creatorcontrib><creatorcontrib>Guevara-Lora, Ibeth</creatorcontrib><creatorcontrib>Bukowski, Michał</creatorcontrib><creatorcontrib>Sabat, Artur J.</creatorcontrib><creatorcontrib>Friedrich, Alexander W.</creatorcontrib><creatorcontrib>Bonar, Emilia</creatorcontrib><creatorcontrib>Międzobrodzki, Jacek</creatorcontrib><creatorcontrib>Dubin, Adam</creatorcontrib><creatorcontrib>Mak, Paweł</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>Publicly Available Content Database</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>Wladyka, Benedykt</au><au>Piejko, Marcin</au><au>Bzowska, Monika</au><au>Pieta, Piotr</au><au>Krzysik, Monika</au><au>Mazurek, Łukasz</au><au>Guevara-Lora, Ibeth</au><au>Bukowski, Michał</au><au>Sabat, Artur J.</au><au>Friedrich, Alexander W.</au><au>Bonar, Emilia</au><au>Międzobrodzki, Jacek</au><au>Dubin, Adam</au><au>Mak, Paweł</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A peptide factor secreted by Staphylococcus pseudintermedius exhibits properties of both bacteriocins and virulence factors</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2015-09-28</date><risdate>2015</risdate><volume>5</volume><issue>1</issue><spage>14569</spage><epage>14569</epage><pages>14569-14569</pages><artnum>14569</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Staphylococcus pseudintermedius
is a common commensal bacterium colonizing the skin and mucosal surfaces of household animals. However, it has recently emerged as a dangerous opportunistic pathogen, comparable to
S. aureus
for humans. The epidemiological situation is further complicated by the increasing number of methicillin-resistant
S. pseudintermedius
infections and evidence of gene transmission driving antibiotic resistance between staphylococci colonizing human and zoonotic hosts. In the present study, we describe a unique peptide, BacSp222, that possesses features characteristic of both bacteriocins and virulence factors. BacSp222 is secreted in high quantities by
S. pseudintermedius
strain 222 isolated from dog skin lesions. This linear, fifty-amino-acid highly cationic peptide is plasmid-encoded and does not exhibit significant sequence similarities to any other known peptides or proteins. BacSp222 kills gram-positive bacteria (at doses ranging from 0.1 to several micromol/l) but also demonstrates significant cytotoxic activities towards eukaryotic cells at slightly higher concentrations. Moreover, at nanomolar concentrations, the peptide also possesses modulatory properties, efficiently enhancing interferon gamma-induced nitric oxide release in murine macrophage-like cell lines. BacSp222 appears to be one of the first examples of multifunctional peptides that breaks the convention of splitting bacteriocins and virulence factors into two unrelated groups.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>26411997</pmid><doi>10.1038/srep14569</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | 13 13/106 14 14/34 14/63 38/22 38/23 38/77 631/1647/2230/2233 631/250/255 631/326/421 631/45/611 64 82/16 82/58 82/81 Amino Acid Sequence Animals Antibiotic resistance Bacteria Bacteriocins Bacteriocins - chemistry Bacteriocins - isolation & purification Bacteriocins - pharmacology Base Sequence Cell Line Cell lines Cell Survival - drug effects Cytotoxicity Drug resistance Gram-positive bacteria Gram-Positive Bacteria - drug effects Humanities and Social Sciences Humans Macrophages Methicillin Microbial Sensitivity Tests Molecular Sequence Data Mucosa multidisciplinary Nitric oxide Nitric Oxide - biosynthesis Nitric Oxide Synthase Type II - metabolism Opportunist infection Peptides Peptides - chemistry Peptides - isolation & purification Peptides - pharmacology Protein Stability Science Sequence Alignment Skin diseases Splitting Staphylococcus - genetics Staphylococcus - metabolism Staphylococcus - pathogenicity Staphylococcus aureus Virulence factors Virulence Factors - chemistry Virulence Factors - isolation & purification Virulence Factors - pharmacology |
title | A peptide factor secreted by Staphylococcus pseudintermedius exhibits properties of both bacteriocins and virulence factors |
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