Lysozyme resistance in Streptococcus suis is highly variable and multifactorial
Streptococcus suis is an important infectious agent for pigs and occasionally for humans. The host innate immune system plays a key role in preventing and eliminating S. suis infections. One important constituent of the innate immune system is the protein lysozyme, which is present in a variety of b...
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| Veröffentlicht in: | PloS one 2012-04, Vol.7 (4), p.e36281-e36281 |
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| description | Streptococcus suis is an important infectious agent for pigs and occasionally for humans. The host innate immune system plays a key role in preventing and eliminating S. suis infections. One important constituent of the innate immune system is the protein lysozyme, which is present in a variety of body fluids and immune cells. Lysozyme acts as a peptidoglycan degrading enzyme causing bacterial lysis. Several pathogens have developed mechanisms to evade lysozyme-mediated killing. In the present study we compared the lysozyme sensitivity of various S. suis isolates and investigated the molecular basis of lysozyme resistance for this pathogen.
The lysozyme minimal inhibitory concentrations of a wide panel of S. suis isolates varied between 0.3 to 10 mg/ml. By inactivating the oatA gene in a serotype 2 and a serotype 9 strain, we showed that OatA-mediated peptidoglycan modification partly contributes to lysozyme resistance. Furthermore, inactivation of the murMN operon provided evidence that additional peptidoglycan crosslinking is not involved in lysozyme resistance in S. suis. Besides a targeted approach, we also used an unbiased approach for identifying factors involved in lysozyme resistance. Based on whole genome comparisons of a lysozyme sensitive strain and selected lysozyme resistant derivatives, we detected several single nucleotide polymorphisms (SNPs) that were correlated with the lysozyme resistance trait. Two SNPs caused defects in protein expression of an autolysin and a capsule sugar transferase. Analysis of specific isogenic mutants, confirmed the involvement of autolysin activity and capsule structures in lysozyme resistance of S. suis.
This study shows that lysozyme resistance levels are highly variable among S. suis isolates and serotypes. Furthermore, the results show that lysozyme resistance in S. suis can involve different mechanisms including OatA-mediated peptidolycan modification, autolysin activity and capsule production. |
| doi_str_mv | 10.1371/journal.pone.0036281 |
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The lysozyme minimal inhibitory concentrations of a wide panel of S. suis isolates varied between 0.3 to 10 mg/ml. By inactivating the oatA gene in a serotype 2 and a serotype 9 strain, we showed that OatA-mediated peptidoglycan modification partly contributes to lysozyme resistance. Furthermore, inactivation of the murMN operon provided evidence that additional peptidoglycan crosslinking is not involved in lysozyme resistance in S. suis. Besides a targeted approach, we also used an unbiased approach for identifying factors involved in lysozyme resistance. Based on whole genome comparisons of a lysozyme sensitive strain and selected lysozyme resistant derivatives, we detected several single nucleotide polymorphisms (SNPs) that were correlated with the lysozyme resistance trait. Two SNPs caused defects in protein expression of an autolysin and a capsule sugar transferase. Analysis of specific isogenic mutants, confirmed the involvement of autolysin activity and capsule structures in lysozyme resistance of S. suis.
This study shows that lysozyme resistance levels are highly variable among S. suis isolates and serotypes. Furthermore, the results show that lysozyme resistance in S. suis can involve different mechanisms including OatA-mediated peptidolycan modification, autolysin activity and capsule production.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0036281</identifier><identifier>PMID: 22558419</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>antibiotic tolerance ; Bacteria ; Bacterial Capsules - genetics ; Bacterial Capsules - metabolism ; Bacteriolysis - genetics ; Biology ; Body fluids ; Chromosomes ; Cloning ; Comparative analysis ; Crosslinking ; deacetylase ; Deactivation ; Endocarditis ; Enzymes ; Genes ; Genes, Bacterial - genetics ; Genomes ; Genomics ; Health aspects ; Immune system ; Immunology ; Inactivation ; Infection ; Infectious diseases ; Innate immunity ; Laboratories ; Lactococcus lactis ; Lysis ; Lysozyme ; Meningitis ; Microbial drug resistance ; Mortality ; Muramidase - metabolism ; murmn operon ; Mutants ; N-Acetylmuramoyl-L-alanine Amidase - genetics ; N-Acetylmuramoyl-L-alanine Amidase - metabolism ; Operon - genetics ; Pathogens ; penicillin resistance ; Peptidoglycan - metabolism ; Peptidoglycans ; pgda gene ; pneumoniae ; Polymorphism, Single Nucleotide ; Proteins ; Resistance factors ; Serotypes ; Single nucleotide polymorphisms ; Single-nucleotide polymorphism ; Staphylococcus aureus ; Streptococcus ; Streptococcus infections ; Streptococcus suis - genetics ; Streptococcus suis - metabolism ; Studies ; Sugar ; Swine ; type-2 ; Veterinary Science ; virulence</subject><ispartof>PloS one, 2012-04, Vol.7 (4), p.e36281-e36281</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012 Wichgers Schreur 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>Wichgers Schreur et al. 2012</rights><rights>Wageningen University & Research</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c776t-362656d3edffc336f33e371cd1e816493448c620b5f755e95d59c26c4ba2d7b83</citedby><cites>FETCH-LOGICAL-c776t-362656d3edffc336f33e371cd1e816493448c620b5f755e95d59c26c4ba2d7b83</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/PMC3340348/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3340348/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22558419$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wichgers Schreur, Paul J</creatorcontrib><creatorcontrib>van Weeghel, Christian</creatorcontrib><creatorcontrib>Rebel, Johanna M J</creatorcontrib><creatorcontrib>Smits, Mari A</creatorcontrib><creatorcontrib>van Putten, Jos P M</creatorcontrib><creatorcontrib>Smith, Hilde E</creatorcontrib><title>Lysozyme resistance in Streptococcus suis is highly variable and multifactorial</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Streptococcus suis is an important infectious agent for pigs and occasionally for humans. The host innate immune system plays a key role in preventing and eliminating S. suis infections. One important constituent of the innate immune system is the protein lysozyme, which is present in a variety of body fluids and immune cells. Lysozyme acts as a peptidoglycan degrading enzyme causing bacterial lysis. Several pathogens have developed mechanisms to evade lysozyme-mediated killing. In the present study we compared the lysozyme sensitivity of various S. suis isolates and investigated the molecular basis of lysozyme resistance for this pathogen.
The lysozyme minimal inhibitory concentrations of a wide panel of S. suis isolates varied between 0.3 to 10 mg/ml. By inactivating the oatA gene in a serotype 2 and a serotype 9 strain, we showed that OatA-mediated peptidoglycan modification partly contributes to lysozyme resistance. Furthermore, inactivation of the murMN operon provided evidence that additional peptidoglycan crosslinking is not involved in lysozyme resistance in S. suis. Besides a targeted approach, we also used an unbiased approach for identifying factors involved in lysozyme resistance. Based on whole genome comparisons of a lysozyme sensitive strain and selected lysozyme resistant derivatives, we detected several single nucleotide polymorphisms (SNPs) that were correlated with the lysozyme resistance trait. Two SNPs caused defects in protein expression of an autolysin and a capsule sugar transferase. Analysis of specific isogenic mutants, confirmed the involvement of autolysin activity and capsule structures in lysozyme resistance of S. suis.
This study shows that lysozyme resistance levels are highly variable among S. suis isolates and serotypes. Furthermore, the results show that lysozyme resistance in S. suis can involve different mechanisms including OatA-mediated peptidolycan modification, autolysin activity and capsule production.</description><subject>antibiotic tolerance</subject><subject>Bacteria</subject><subject>Bacterial Capsules - genetics</subject><subject>Bacterial Capsules - metabolism</subject><subject>Bacteriolysis - genetics</subject><subject>Biology</subject><subject>Body fluids</subject><subject>Chromosomes</subject><subject>Cloning</subject><subject>Comparative analysis</subject><subject>Crosslinking</subject><subject>deacetylase</subject><subject>Deactivation</subject><subject>Endocarditis</subject><subject>Enzymes</subject><subject>Genes</subject><subject>Genes, Bacterial - genetics</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Health aspects</subject><subject>Immune system</subject><subject>Immunology</subject><subject>Inactivation</subject><subject>Infection</subject><subject>Infectious diseases</subject><subject>Innate immunity</subject><subject>Laboratories</subject><subject>Lactococcus lactis</subject><subject>Lysis</subject><subject>Lysozyme</subject><subject>Meningitis</subject><subject>Microbial drug resistance</subject><subject>Mortality</subject><subject>Muramidase - metabolism</subject><subject>murmn operon</subject><subject>Mutants</subject><subject>N-Acetylmuramoyl-L-alanine Amidase - genetics</subject><subject>N-Acetylmuramoyl-L-alanine Amidase - metabolism</subject><subject>Operon - genetics</subject><subject>Pathogens</subject><subject>penicillin resistance</subject><subject>Peptidoglycan - metabolism</subject><subject>Peptidoglycans</subject><subject>pgda gene</subject><subject>pneumoniae</subject><subject>Polymorphism, Single Nucleotide</subject><subject>Proteins</subject><subject>Resistance factors</subject><subject>Serotypes</subject><subject>Single nucleotide polymorphisms</subject><subject>Single-nucleotide polymorphism</subject><subject>Staphylococcus aureus</subject><subject>Streptococcus</subject><subject>Streptococcus infections</subject><subject>Streptococcus suis - genetics</subject><subject>Streptococcus suis - metabolism</subject><subject>Studies</subject><subject>Sugar</subject><subject>Swine</subject><subject>type-2</subject><subject>Veterinary Science</subject><subject>virulence</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNk12L1DAUhoso7rr6D0QLgujFjE2Tpo0XwrL4MTAw4Kq3IU1POxkyyWyS7jr-etOd7jKVvZCWppw-79tzTnKS5CXK5giX6MPG9s4IPd9ZA_MswzSv0KPkFDGcz2ie4cdH7yfJM-83WVbgitKnyUmeF0VFEDtNVsu9t3_2W0gdeOWDMBJSZdLL4GAXrLRS9j71vfJpvNeqW-t9ei2cErWGVJgm3fY6qFbIYGNQP0-etEJ7eDGuZ8nPL59_XHybLVdfFxfny5ksSxpmMVta0AZD07YSY9piDLEo2SCoECUME1LJmHldtGVRACuagsmcSlKLvCnrCp8lrw--O209H3vhOcI5iaVlZRmJxYForNjwnVNb4fbcCsVvA9Z1XLigpAZe5ZjKGjFJBSUZFqypoEVQ5ILJklZF9Pp48LoRHRhl4oMb4aTyt4Za1W4wv-kdN3pYdn3tOclJ1EbxpzHVvt5CI8EEJ_Qko-kXo9a8s9cc45gMGWp9Nxo4e9WDD3yrvASthQHbx6IzhBCL-zkk-uYf9OHWjFQnYvXKtDb-Vw6m_JyUlDEWNyFS8weoeDWwVTKeulbF-ETwfiKITIDfoRO993xx-f3_2dWvKfv2iF2D0GHtre6DssZPQXIApbPeO2jvm4wyPgzNXTf4MDR8HJooe3W8QfeiuynBfwE10BNl</recordid><startdate>20120430</startdate><enddate>20120430</enddate><creator>Wichgers Schreur, Paul J</creator><creator>van Weeghel, Christian</creator><creator>Rebel, Johanna M J</creator><creator>Smits, Mari A</creator><creator>van Putten, Jos P M</creator><creator>Smith, Hilde E</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>QVL</scope><scope>DOA</scope></search><sort><creationdate>20120430</creationdate><title>Lysozyme resistance in Streptococcus suis is highly variable and multifactorial</title><author>Wichgers Schreur, Paul J ; van Weeghel, Christian ; Rebel, Johanna M J ; Smits, Mari A ; van Putten, Jos P M ; Smith, Hilde E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c776t-362656d3edffc336f33e371cd1e816493448c620b5f755e95d59c26c4ba2d7b83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>antibiotic tolerance</topic><topic>Bacteria</topic><topic>Bacterial Capsules - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>NARCIS:Publications</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wichgers Schreur, Paul J</au><au>van Weeghel, Christian</au><au>Rebel, Johanna M J</au><au>Smits, Mari A</au><au>van Putten, Jos P M</au><au>Smith, Hilde E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lysozyme resistance in Streptococcus suis is highly variable and multifactorial</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2012-04-30</date><risdate>2012</risdate><volume>7</volume><issue>4</issue><spage>e36281</spage><epage>e36281</epage><pages>e36281-e36281</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Streptococcus suis is an important infectious agent for pigs and occasionally for humans. The host innate immune system plays a key role in preventing and eliminating S. suis infections. One important constituent of the innate immune system is the protein lysozyme, which is present in a variety of body fluids and immune cells. Lysozyme acts as a peptidoglycan degrading enzyme causing bacterial lysis. Several pathogens have developed mechanisms to evade lysozyme-mediated killing. In the present study we compared the lysozyme sensitivity of various S. suis isolates and investigated the molecular basis of lysozyme resistance for this pathogen.
The lysozyme minimal inhibitory concentrations of a wide panel of S. suis isolates varied between 0.3 to 10 mg/ml. By inactivating the oatA gene in a serotype 2 and a serotype 9 strain, we showed that OatA-mediated peptidoglycan modification partly contributes to lysozyme resistance. Furthermore, inactivation of the murMN operon provided evidence that additional peptidoglycan crosslinking is not involved in lysozyme resistance in S. suis. Besides a targeted approach, we also used an unbiased approach for identifying factors involved in lysozyme resistance. Based on whole genome comparisons of a lysozyme sensitive strain and selected lysozyme resistant derivatives, we detected several single nucleotide polymorphisms (SNPs) that were correlated with the lysozyme resistance trait. Two SNPs caused defects in protein expression of an autolysin and a capsule sugar transferase. Analysis of specific isogenic mutants, confirmed the involvement of autolysin activity and capsule structures in lysozyme resistance of S. suis.
This study shows that lysozyme resistance levels are highly variable among S. suis isolates and serotypes. Furthermore, the results show that lysozyme resistance in S. suis can involve different mechanisms including OatA-mediated peptidolycan modification, autolysin activity and capsule production.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22558419</pmid><doi>10.1371/journal.pone.0036281</doi><tpages>e36281</tpages><oa>free_for_read</oa></addata></record> |
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| recordid | cdi_plos_journals_1324558077 |
| source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | antibiotic tolerance Bacteria Bacterial Capsules - genetics Bacterial Capsules - metabolism Bacteriolysis - genetics Biology Body fluids Chromosomes Cloning Comparative analysis Crosslinking deacetylase Deactivation Endocarditis Enzymes Genes Genes, Bacterial - genetics Genomes Genomics Health aspects Immune system Immunology Inactivation Infection Infectious diseases Innate immunity Laboratories Lactococcus lactis Lysis Lysozyme Meningitis Microbial drug resistance Mortality Muramidase - metabolism murmn operon Mutants N-Acetylmuramoyl-L-alanine Amidase - genetics N-Acetylmuramoyl-L-alanine Amidase - metabolism Operon - genetics Pathogens penicillin resistance Peptidoglycan - metabolism Peptidoglycans pgda gene pneumoniae Polymorphism, Single Nucleotide Proteins Resistance factors Serotypes Single nucleotide polymorphisms Single-nucleotide polymorphism Staphylococcus aureus Streptococcus Streptococcus infections Streptococcus suis - genetics Streptococcus suis - metabolism Studies Sugar Swine type-2 Veterinary Science virulence |
| title | Lysozyme resistance in Streptococcus suis is highly variable and multifactorial |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T07%3A25%3A02IST&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=Lysozyme%20resistance%20in%20Streptococcus%20suis%20is%20highly%20variable%20and%20multifactorial&rft.jtitle=PloS%20one&rft.au=Wichgers%20Schreur,%20Paul%20J&rft.date=2012-04-30&rft.volume=7&rft.issue=4&rft.spage=e36281&rft.epage=e36281&rft.pages=e36281-e36281&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0036281&rft_dat=%3Cgale_plos_%3EA476999816%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=1324558077&rft_id=info:pmid/22558419&rft_galeid=A476999816&rft_doaj_id=oai_doaj_org_article_8236cb19c6a6403a9d8ef1e52a9c7685&rfr_iscdi=true |