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Effect of interactions between Mip and PrtA on the full extracellular protease activity of Xanthomonas campestris pathovar campestris
Abstract Mip (macrophage infectivity potentiator) and Mip-like proteins have been demonstrated to be involved in virulence of several animal pathogens, but as yet none of their native bacterial targets has been identified. Our previous work demonstrated that the Mip-like protein found in the plant p...
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| Published in: | FEMS microbiology letters 2011-10, Vol.323 (2), p.180-187 |
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| creator | Meng, Qing-Lin Tang, Dong-Jie Fan, Ying-Yuan Li, Zhen-Jiang Zhang, Hui He, Yong-Qiang Jiang, Bo-Le Lu, Guang-Tao Tang, Ji-Liang |
| description | Abstract
Mip (macrophage infectivity potentiator) and Mip-like proteins have been demonstrated to be involved in virulence of several animal pathogens, but as yet none of their native bacterial targets has been identified. Our previous work demonstrated that the Mip-like protein found in the plant pathogen anthomonas campestris pv. campestris ( ) (hereafter called MipXcc) is also involved in virulence. Inactivation of the gene leads to a significant reduction in exopolysaccharide production and extracellular protease activity via an unknown mechanism. The genome encodes six extracellular proteases, all of which are secreted via the type II secretion system. The serine protease PrtA makes the largest contribution to 's total extracellular proteolytic activity. In this study, Western blotting analysis demonstrated that MipXcc was located in the periplasm. Bacterial two-hybrid and far-Western analysis indicated that MipXcc interacted with PrtA directly. Purified MipXcc was found to be able to rescue the protease activity of periplasmic proteins extracted from the mutant. These findings show that MipXcc plays a role in the maturation of PrtA, which is the novel native target for at least one Mip or Mip-like protein. |
| doi_str_mv | 10.1111/j.1574-6968.2011.02377.x |
| format | article |
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Mip (macrophage infectivity potentiator) and Mip-like proteins have been demonstrated to be involved in virulence of several animal pathogens, but as yet none of their native bacterial targets has been identified. Our previous work demonstrated that the Mip-like protein found in the plant pathogen anthomonas campestris pv. campestris ( ) (hereafter called MipXcc) is also involved in virulence. Inactivation of the gene leads to a significant reduction in exopolysaccharide production and extracellular protease activity via an unknown mechanism. The genome encodes six extracellular proteases, all of which are secreted via the type II secretion system. The serine protease PrtA makes the largest contribution to 's total extracellular proteolytic activity. In this study, Western blotting analysis demonstrated that MipXcc was located in the periplasm. Bacterial two-hybrid and far-Western analysis indicated that MipXcc interacted with PrtA directly. Purified MipXcc was found to be able to rescue the protease activity of periplasmic proteins extracted from the mutant. These findings show that MipXcc plays a role in the maturation of PrtA, which is the novel native target for at least one Mip or Mip-like protein.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2011.02377.x</identifier><identifier>PMID: 22092718</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Bacterial plant pathogens ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Blotting, Far-Western ; Blotting, Western ; Deactivation ; Exopolysaccharides ; extracellular protease ; Fundamental and applied biological sciences. Psychology ; Gene Knockout Techniques ; Genomes ; Inactivation ; Infectivity ; Macrophages ; Microbiology ; mip‐like ; Miscellaneous ; Pathogens ; Peptide Hydrolases - genetics ; Peptide Hydrolases - metabolism ; Periplasm ; periplasmic PPIase ; Periplasmic Proteins - genetics ; Periplasmic Proteins - metabolism ; Phytopathology. Animal pests. Plant and forest protection ; Protease ; Protein Binding ; Protein Interaction Mapping ; Proteins ; Proteolysis ; PrtA ; Secretion ; Serine ; Serine proteinase ; Target recognition ; Two-Hybrid System Techniques ; Virulence ; Virulence Factors - genetics ; Virulence Factors - metabolism ; Western blotting ; Xanthomonas ; Xanthomonas campestris ; Xanthomonas campestris - enzymology ; Xanthomonas campestris - genetics</subject><ispartof>FEMS microbiology letters, 2011-10, Vol.323 (2), p.180-187</ispartof><rights>2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved 2011</rights><rights>2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved</rights><rights>2015 INIST-CNRS</rights><rights>2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5537-340344203bbafc236e6e0abfc9826c98e947dc68fe6b0d667fbfa08bfc0e598b3</citedby><cites>FETCH-LOGICAL-c5537-340344203bbafc236e6e0abfc9826c98e947dc68fe6b0d667fbfa08bfc0e598b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24567036$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22092718$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meng, Qing-Lin</creatorcontrib><creatorcontrib>Tang, Dong-Jie</creatorcontrib><creatorcontrib>Fan, Ying-Yuan</creatorcontrib><creatorcontrib>Li, Zhen-Jiang</creatorcontrib><creatorcontrib>Zhang, Hui</creatorcontrib><creatorcontrib>He, Yong-Qiang</creatorcontrib><creatorcontrib>Jiang, Bo-Le</creatorcontrib><creatorcontrib>Lu, Guang-Tao</creatorcontrib><creatorcontrib>Tang, Ji-Liang</creatorcontrib><title>Effect of interactions between Mip and PrtA on the full extracellular protease activity of Xanthomonas campestris pathovar campestris</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
Mip (macrophage infectivity potentiator) and Mip-like proteins have been demonstrated to be involved in virulence of several animal pathogens, but as yet none of their native bacterial targets has been identified. Our previous work demonstrated that the Mip-like protein found in the plant pathogen anthomonas campestris pv. campestris ( ) (hereafter called MipXcc) is also involved in virulence. Inactivation of the gene leads to a significant reduction in exopolysaccharide production and extracellular protease activity via an unknown mechanism. The genome encodes six extracellular proteases, all of which are secreted via the type II secretion system. The serine protease PrtA makes the largest contribution to 's total extracellular proteolytic activity. In this study, Western blotting analysis demonstrated that MipXcc was located in the periplasm. Bacterial two-hybrid and far-Western analysis indicated that MipXcc interacted with PrtA directly. Purified MipXcc was found to be able to rescue the protease activity of periplasmic proteins extracted from the mutant. These findings show that MipXcc plays a role in the maturation of PrtA, which is the novel native target for at least one Mip or Mip-like protein.</description><subject>Bacterial plant pathogens</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Blotting, Far-Western</subject><subject>Blotting, Western</subject><subject>Deactivation</subject><subject>Exopolysaccharides</subject><subject>extracellular protease</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Knockout Techniques</subject><subject>Genomes</subject><subject>Inactivation</subject><subject>Infectivity</subject><subject>Macrophages</subject><subject>Microbiology</subject><subject>mip‐like</subject><subject>Miscellaneous</subject><subject>Pathogens</subject><subject>Peptide Hydrolases - genetics</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Periplasm</subject><subject>periplasmic PPIase</subject><subject>Periplasmic Proteins - genetics</subject><subject>Periplasmic Proteins - metabolism</subject><subject>Phytopathology. Animal pests. Plant and forest protection</subject><subject>Protease</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>PrtA</subject><subject>Secretion</subject><subject>Serine</subject><subject>Serine proteinase</subject><subject>Target recognition</subject><subject>Two-Hybrid System Techniques</subject><subject>Virulence</subject><subject>Virulence Factors - genetics</subject><subject>Virulence Factors - metabolism</subject><subject>Western blotting</subject><subject>Xanthomonas</subject><subject>Xanthomonas campestris</subject><subject>Xanthomonas campestris - enzymology</subject><subject>Xanthomonas campestris - genetics</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNqNkcuKFDEUhoMoTjv6ChIQ0U2VJ5WqXBYuhmFGhR50oeAupKpPmGrqZpKa6X4A39uU3c6AophFcjj5_nPhJ4QyyFk6b7Y5q2SZCS1UXgBjORRcynz3gKzuPh6SFXCpMgZanpAnIWwBoCxAPCYnRQG6kEytyPcL57CJdHS0HSJ628R2HAKtMd4iDvSqnagdNvSTj2d0HGi8RurmrqO4iwnGrps76-nkx4g2IF30N23cLwW_2iFej_042EAb208Yom8DnWzK3iTRfe4peeRsF_DZ8T0lXy4vPp-_z9Yf3304P1tnTVVxmfESeJlW4HVtXVNwgQLB1q7RqhDpQl3KTSOUQ1HDRgjpamdBJQCw0qrmp-TVoW6a99ucepu-DcsSdsBxDkZDJYQGzRP5-p8k46UqFSuZTOiL39DtOPsh7WEKDpVSUoNKlDpQjR9D8OjM5Nve-r1hYBZTzdYs3pnFO7OYan6aanZJ-vzYYK573NwJf7mYgJdHwIbGds7boWnDPVdWQgIXiXt74G7bDvf_PYC5vFovUdLzg36cp7-osz_H_wGTbM4_</recordid><startdate>201110</startdate><enddate>201110</enddate><creator>Meng, Qing-Lin</creator><creator>Tang, Dong-Jie</creator><creator>Fan, Ying-Yuan</creator><creator>Li, Zhen-Jiang</creator><creator>Zhang, Hui</creator><creator>He, Yong-Qiang</creator><creator>Jiang, Bo-Le</creator><creator>Lu, Guang-Tao</creator><creator>Tang, Ji-Liang</creator><general>Blackwell Publishing Ltd</general><general>Wiley-Blackwell</general><general>Oxford University Press</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</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>C1K</scope><scope>CCPQU</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>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>201110</creationdate><title>Effect of interactions between Mip and PrtA on the full extracellular protease activity of Xanthomonas campestris pathovar campestris</title><author>Meng, Qing-Lin ; Tang, Dong-Jie ; Fan, Ying-Yuan ; Li, Zhen-Jiang ; Zhang, Hui ; He, Yong-Qiang ; Jiang, Bo-Le ; Lu, Guang-Tao ; Tang, Ji-Liang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5537-340344203bbafc236e6e0abfc9826c98e947dc68fe6b0d667fbfa08bfc0e598b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Bacterial plant pathogens</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Blotting, Far-Western</topic><topic>Blotting, Western</topic><topic>Deactivation</topic><topic>Exopolysaccharides</topic><topic>extracellular protease</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Knockout Techniques</topic><topic>Genomes</topic><topic>Inactivation</topic><topic>Infectivity</topic><topic>Macrophages</topic><topic>Microbiology</topic><topic>mip‐like</topic><topic>Miscellaneous</topic><topic>Pathogens</topic><topic>Peptide Hydrolases - genetics</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Periplasm</topic><topic>periplasmic PPIase</topic><topic>Periplasmic Proteins - genetics</topic><topic>Periplasmic Proteins - metabolism</topic><topic>Phytopathology. Animal pests. Plant and forest protection</topic><topic>Protease</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>PrtA</topic><topic>Secretion</topic><topic>Serine</topic><topic>Serine proteinase</topic><topic>Target recognition</topic><topic>Two-Hybrid System Techniques</topic><topic>Virulence</topic><topic>Virulence Factors - genetics</topic><topic>Virulence Factors - metabolism</topic><topic>Western blotting</topic><topic>Xanthomonas</topic><topic>Xanthomonas campestris</topic><topic>Xanthomonas campestris - enzymology</topic><topic>Xanthomonas campestris - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meng, Qing-Lin</creatorcontrib><creatorcontrib>Tang, Dong-Jie</creatorcontrib><creatorcontrib>Fan, Ying-Yuan</creatorcontrib><creatorcontrib>Li, Zhen-Jiang</creatorcontrib><creatorcontrib>Zhang, Hui</creatorcontrib><creatorcontrib>He, Yong-Qiang</creatorcontrib><creatorcontrib>Jiang, Bo-Le</creatorcontrib><creatorcontrib>Lu, Guang-Tao</creatorcontrib><creatorcontrib>Tang, Ji-Liang</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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</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)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</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 China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meng, Qing-Lin</au><au>Tang, Dong-Jie</au><au>Fan, Ying-Yuan</au><au>Li, Zhen-Jiang</au><au>Zhang, Hui</au><au>He, Yong-Qiang</au><au>Jiang, Bo-Le</au><au>Lu, Guang-Tao</au><au>Tang, Ji-Liang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of interactions between Mip and PrtA on the full extracellular protease activity of Xanthomonas campestris pathovar campestris</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2011-10</date><risdate>2011</risdate><volume>323</volume><issue>2</issue><spage>180</spage><epage>187</epage><pages>180-187</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-1</notes><notes>content type line 23</notes><notes>ObjectType-Article-1</notes><notes>ObjectType-Feature-2</notes><abstract>Abstract
Mip (macrophage infectivity potentiator) and Mip-like proteins have been demonstrated to be involved in virulence of several animal pathogens, but as yet none of their native bacterial targets has been identified. Our previous work demonstrated that the Mip-like protein found in the plant pathogen anthomonas campestris pv. campestris ( ) (hereafter called MipXcc) is also involved in virulence. Inactivation of the gene leads to a significant reduction in exopolysaccharide production and extracellular protease activity via an unknown mechanism. The genome encodes six extracellular proteases, all of which are secreted via the type II secretion system. The serine protease PrtA makes the largest contribution to 's total extracellular proteolytic activity. In this study, Western blotting analysis demonstrated that MipXcc was located in the periplasm. Bacterial two-hybrid and far-Western analysis indicated that MipXcc interacted with PrtA directly. Purified MipXcc was found to be able to rescue the protease activity of periplasmic proteins extracted from the mutant. These findings show that MipXcc plays a role in the maturation of PrtA, which is the novel native target for at least one Mip or Mip-like protein.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>22092718</pmid><doi>10.1111/j.1574-6968.2011.02377.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | Oxford Journals - Connect here FIRST to enable access |
| subjects | Bacterial plant pathogens Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Blotting, Far-Western Blotting, Western Deactivation Exopolysaccharides extracellular protease Fundamental and applied biological sciences. Psychology Gene Knockout Techniques Genomes Inactivation Infectivity Macrophages Microbiology mip‐like Miscellaneous Pathogens Peptide Hydrolases - genetics Peptide Hydrolases - metabolism Periplasm periplasmic PPIase Periplasmic Proteins - genetics Periplasmic Proteins - metabolism Phytopathology. Animal pests. Plant and forest protection Protease Protein Binding Protein Interaction Mapping Proteins Proteolysis PrtA Secretion Serine Serine proteinase Target recognition Two-Hybrid System Techniques Virulence Virulence Factors - genetics Virulence Factors - metabolism Western blotting Xanthomonas Xanthomonas campestris Xanthomonas campestris - enzymology Xanthomonas campestris - genetics |
| title | Effect of interactions between Mip and PrtA on the full extracellular protease activity of Xanthomonas campestris pathovar campestris |
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