PerR controls Mn‐dependent resistance to oxidative stress in Neisseria gonorrhoeae
Summary In previous studies it has been established that resistance to superoxide by Neisseria gonorrhoeae is dependent on the accumulation of Mn(II) ions involving the ABC transporter, MntABC. A mutant strain lacking the periplasmic binding protein component (MntC) of this transport system is hyper...
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| Veröffentlicht in: | Molecular microbiology 2006-04, Vol.60 (2), p.401-416 |
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| creator | Wu, Hsing‐Ju Seib, Kate L. Srikhanta, Yogitha N. Kidd, Stephen P. Edwards, Jennifer L. Maguire, Tina L. Grimmond, Sean M. Apicella, Michael A. McEwan, Alastair G. Jennings, Michael P. |
| description | Summary
In previous studies it has been established that resistance to superoxide by Neisseria gonorrhoeae is dependent on the accumulation of Mn(II) ions involving the ABC transporter, MntABC. A mutant strain lacking the periplasmic binding protein component (MntC) of this transport system is hypersensitive to killing by superoxide anion. In this study the mntC mutant was found to be more sensitive to H2O2 killing than the wild‐type. Analysis of regulation of MntC expression revealed that it was de‐repressed under low Mn(II) conditions. The N. gonorrhoeae mntABC locus lacks the mntR repressor typically found associated with this locus in other organisms. A search for a candidate regulator of mntABC expression revealed a homologue of PerR, a Mn‐dependent peroxide‐responsive regulator found in Gram‐positive organisms. A perR mutant expressed more MntC protein than wild‐type, and expression was independent of Mn(II), consistent with a role for PerR as a repressor of mntABC expression. The PerR regulon of N. gonorrhoeae was defined by microarray analysis and includes ribosomal proteins, TonB‐dependent receptors and an alcohol dehydrogenase. Both the mntC and perR mutants had reduced intracellular survival in a human cervical epithelial cell model. |
| doi_str_mv | 10.1111/j.1365-2958.2006.05079.x |
| format | Article |
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In previous studies it has been established that resistance to superoxide by Neisseria gonorrhoeae is dependent on the accumulation of Mn(II) ions involving the ABC transporter, MntABC. A mutant strain lacking the periplasmic binding protein component (MntC) of this transport system is hypersensitive to killing by superoxide anion. In this study the mntC mutant was found to be more sensitive to H2O2 killing than the wild‐type. Analysis of regulation of MntC expression revealed that it was de‐repressed under low Mn(II) conditions. The N. gonorrhoeae mntABC locus lacks the mntR repressor typically found associated with this locus in other organisms. A search for a candidate regulator of mntABC expression revealed a homologue of PerR, a Mn‐dependent peroxide‐responsive regulator found in Gram‐positive organisms. A perR mutant expressed more MntC protein than wild‐type, and expression was independent of Mn(II), consistent with a role for PerR as a repressor of mntABC expression. The PerR regulon of N. gonorrhoeae was defined by microarray analysis and includes ribosomal proteins, TonB‐dependent receptors and an alcohol dehydrogenase. Both the mntC and perR mutants had reduced intracellular survival in a human cervical epithelial cell model.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2006.05079.x</identifier><identifier>PMID: 16573689</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Bacterial Proteins - genetics ; Bacterial Proteins - physiology ; Bacteriology ; Biological and medical sciences ; Catalase - metabolism ; Drug Resistance, Bacterial - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Expression Profiling ; Gene Expression Regulation, Bacterial ; Hydrogen Peroxide - toxicity ; Manganese - metabolism ; Manganese compounds ; Microbiology ; Microorganisms ; Miscellaneous ; Neisseria gonorrhoeae ; Neisseria gonorrhoeae - chemistry ; Neisseria gonorrhoeae - genetics ; Neisseria gonorrhoeae - metabolism ; Oligonucleotide Array Sequence Analysis ; Oxidative Stress - genetics ; Oxygen ; Periplasmic Binding Proteins - analysis ; Periplasmic Binding Proteins - genetics ; Periplasmic Binding Proteins - metabolism ; Proteins ; Regulon - genetics ; Repressor Proteins - genetics ; Repressor Proteins - physiology ; Transcription Factors - genetics ; Transcription Factors - physiology</subject><ispartof>Molecular microbiology, 2006-04, Vol.60 (2), p.401-416</ispartof><rights>2006 INIST-CNRS</rights><rights>Copyright Blackwell Publishing Apr 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5109-12a310e8630a53cb303a8ffc08e14bfe0f0af844aa8b58efbf4bbb044aff8ab93</citedby><cites>FETCH-LOGICAL-c5109-12a310e8630a53cb303a8ffc08e14bfe0f0af844aa8b58efbf4bbb044aff8ab93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2958.2006.05079.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.2006.05079.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27903,27904,45553,45554,46388,46812</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17629998$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16573689$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wu, Hsing‐Ju</creatorcontrib><creatorcontrib>Seib, Kate L.</creatorcontrib><creatorcontrib>Srikhanta, Yogitha N.</creatorcontrib><creatorcontrib>Kidd, Stephen P.</creatorcontrib><creatorcontrib>Edwards, Jennifer L.</creatorcontrib><creatorcontrib>Maguire, Tina L.</creatorcontrib><creatorcontrib>Grimmond, Sean M.</creatorcontrib><creatorcontrib>Apicella, Michael A.</creatorcontrib><creatorcontrib>McEwan, Alastair G.</creatorcontrib><creatorcontrib>Jennings, Michael P.</creatorcontrib><title>PerR controls Mn‐dependent resistance to oxidative stress in Neisseria gonorrhoeae</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
In previous studies it has been established that resistance to superoxide by Neisseria gonorrhoeae is dependent on the accumulation of Mn(II) ions involving the ABC transporter, MntABC. A mutant strain lacking the periplasmic binding protein component (MntC) of this transport system is hypersensitive to killing by superoxide anion. In this study the mntC mutant was found to be more sensitive to H2O2 killing than the wild‐type. Analysis of regulation of MntC expression revealed that it was de‐repressed under low Mn(II) conditions. The N. gonorrhoeae mntABC locus lacks the mntR repressor typically found associated with this locus in other organisms. A search for a candidate regulator of mntABC expression revealed a homologue of PerR, a Mn‐dependent peroxide‐responsive regulator found in Gram‐positive organisms. A perR mutant expressed more MntC protein than wild‐type, and expression was independent of Mn(II), consistent with a role for PerR as a repressor of mntABC expression. The PerR regulon of N. gonorrhoeae was defined by microarray analysis and includes ribosomal proteins, TonB‐dependent receptors and an alcohol dehydrogenase. Both the mntC and perR mutants had reduced intracellular survival in a human cervical epithelial cell model.</description><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - physiology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Catalase - metabolism</subject><subject>Drug Resistance, Bacterial - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Profiling</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Hydrogen Peroxide - toxicity</subject><subject>Manganese - metabolism</subject><subject>Manganese compounds</subject><subject>Microbiology</subject><subject>Microorganisms</subject><subject>Miscellaneous</subject><subject>Neisseria gonorrhoeae</subject><subject>Neisseria gonorrhoeae - chemistry</subject><subject>Neisseria gonorrhoeae - genetics</subject><subject>Neisseria gonorrhoeae - metabolism</subject><subject>Oligonucleotide Array Sequence Analysis</subject><subject>Oxidative Stress - genetics</subject><subject>Oxygen</subject><subject>Periplasmic Binding Proteins - analysis</subject><subject>Periplasmic Binding Proteins - genetics</subject><subject>Periplasmic Binding Proteins - metabolism</subject><subject>Proteins</subject><subject>Regulon - genetics</subject><subject>Repressor Proteins - genetics</subject><subject>Repressor Proteins - physiology</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - physiology</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkFFrFDEQgINY7LX6FyQI-rbrZHPZTR58kNLWQk9FKvgWkr2J5thLzmTPXt_8Cf2N_hKz3mHBJwNDhplvhuEjhDKoWXmvVzXjragaJWTdALQ1COhUvXtEZn8bj8kMlICKy-bLMTnJeQXAOLT8CTlmreh4K9WM3HzE9In2MYwpDpkuwq-f90vcYFhiGGnC7PNoQo90jDTu_NKM_gfSPJZOpj7Q9-hzxuQN_RpDTOlbRINPyZEzQ8Znh_-UfL44vzl7V11_uLw6e3td9YKBqlhjOAOULQcjeG85cCOd60Eim1uH4MA4OZ8bI62Q6KybW2uhFJyTxip-Sl7t925S_L7FPOq1zz0OgwkYt1mzrgEpuq6AL_4BV3GbQrlNM9WKEg0vkNxDfYo5J3R6k_zapDvNQE_a9UpPdvVkV0_a9R_teldGnx_2b-0alw-DB88FeHkATO7N4FJx6vMD17WNUkoW7s2eu_UD3v33AXqxuJoy_hvEOqAq</recordid><startdate>200604</startdate><enddate>200604</enddate><creator>Wu, Hsing‐Ju</creator><creator>Seib, Kate L.</creator><creator>Srikhanta, Yogitha N.</creator><creator>Kidd, Stephen P.</creator><creator>Edwards, Jennifer L.</creator><creator>Maguire, Tina L.</creator><creator>Grimmond, Sean M.</creator><creator>Apicella, Michael A.</creator><creator>McEwan, Alastair G.</creator><creator>Jennings, Michael P.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell Science</general><scope>IQODW</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>200604</creationdate><title>PerR controls Mn‐dependent resistance to oxidative stress in Neisseria gonorrhoeae</title><author>Wu, Hsing‐Ju ; Seib, Kate L. ; Srikhanta, Yogitha N. ; Kidd, Stephen P. ; Edwards, Jennifer L. ; Maguire, Tina L. ; Grimmond, Sean M. ; Apicella, Michael A. ; McEwan, Alastair G. ; Jennings, Michael P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5109-12a310e8630a53cb303a8ffc08e14bfe0f0af844aa8b58efbf4bbb044aff8ab93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - physiology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Catalase - metabolism</topic><topic>Drug Resistance, Bacterial - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Profiling</topic><topic>Gene Expression Regulation, Bacterial</topic><topic>Hydrogen Peroxide - toxicity</topic><topic>Manganese - metabolism</topic><topic>Manganese compounds</topic><topic>Microbiology</topic><topic>Microorganisms</topic><topic>Miscellaneous</topic><topic>Neisseria gonorrhoeae</topic><topic>Neisseria gonorrhoeae - chemistry</topic><topic>Neisseria gonorrhoeae - genetics</topic><topic>Neisseria gonorrhoeae - metabolism</topic><topic>Oligonucleotide Array Sequence Analysis</topic><topic>Oxidative Stress - genetics</topic><topic>Oxygen</topic><topic>Periplasmic Binding Proteins - analysis</topic><topic>Periplasmic Binding Proteins - genetics</topic><topic>Periplasmic Binding Proteins - metabolism</topic><topic>Proteins</topic><topic>Regulon - genetics</topic><topic>Repressor Proteins - genetics</topic><topic>Repressor Proteins - physiology</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, Hsing‐Ju</creatorcontrib><creatorcontrib>Seib, Kate L.</creatorcontrib><creatorcontrib>Srikhanta, Yogitha N.</creatorcontrib><creatorcontrib>Kidd, Stephen P.</creatorcontrib><creatorcontrib>Edwards, Jennifer L.</creatorcontrib><creatorcontrib>Maguire, Tina L.</creatorcontrib><creatorcontrib>Grimmond, Sean M.</creatorcontrib><creatorcontrib>Apicella, Michael A.</creatorcontrib><creatorcontrib>McEwan, Alastair G.</creatorcontrib><creatorcontrib>Jennings, Michael P.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, Hsing‐Ju</au><au>Seib, Kate L.</au><au>Srikhanta, Yogitha N.</au><au>Kidd, Stephen P.</au><au>Edwards, Jennifer L.</au><au>Maguire, Tina L.</au><au>Grimmond, Sean M.</au><au>Apicella, Michael A.</au><au>McEwan, Alastair G.</au><au>Jennings, Michael P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PerR controls Mn‐dependent resistance to oxidative stress in Neisseria gonorrhoeae</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2006-04</date><risdate>2006</risdate><volume>60</volume><issue>2</issue><spage>401</spage><epage>416</epage><pages>401-416</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
In previous studies it has been established that resistance to superoxide by Neisseria gonorrhoeae is dependent on the accumulation of Mn(II) ions involving the ABC transporter, MntABC. A mutant strain lacking the periplasmic binding protein component (MntC) of this transport system is hypersensitive to killing by superoxide anion. In this study the mntC mutant was found to be more sensitive to H2O2 killing than the wild‐type. Analysis of regulation of MntC expression revealed that it was de‐repressed under low Mn(II) conditions. The N. gonorrhoeae mntABC locus lacks the mntR repressor typically found associated with this locus in other organisms. A search for a candidate regulator of mntABC expression revealed a homologue of PerR, a Mn‐dependent peroxide‐responsive regulator found in Gram‐positive organisms. A perR mutant expressed more MntC protein than wild‐type, and expression was independent of Mn(II), consistent with a role for PerR as a repressor of mntABC expression. The PerR regulon of N. gonorrhoeae was defined by microarray analysis and includes ribosomal proteins, TonB‐dependent receptors and an alcohol dehydrogenase. Both the mntC and perR mutants had reduced intracellular survival in a human cervical epithelial cell model.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>16573689</pmid><doi>10.1111/j.1365-2958.2006.05079.x</doi><tpages>16</tpages></addata></record> |
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| subjects | Bacterial Proteins - genetics Bacterial Proteins - physiology Bacteriology Biological and medical sciences Catalase - metabolism Drug Resistance, Bacterial - genetics Fundamental and applied biological sciences. Psychology Gene Expression Profiling Gene Expression Regulation, Bacterial Hydrogen Peroxide - toxicity Manganese - metabolism Manganese compounds Microbiology Microorganisms Miscellaneous Neisseria gonorrhoeae Neisseria gonorrhoeae - chemistry Neisseria gonorrhoeae - genetics Neisseria gonorrhoeae - metabolism Oligonucleotide Array Sequence Analysis Oxidative Stress - genetics Oxygen Periplasmic Binding Proteins - analysis Periplasmic Binding Proteins - genetics Periplasmic Binding Proteins - metabolism Proteins Regulon - genetics Repressor Proteins - genetics Repressor Proteins - physiology Transcription Factors - genetics Transcription Factors - physiology |
| title | PerR controls Mn‐dependent resistance to oxidative stress in Neisseria gonorrhoeae |
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