A proteomic study of Escherichia coli O157:H7 NCTC 12900 cultivated in biofilm or in planktonic growth mode
Abstract Escherichia coli 0157:H7 biofilms were studied by a new method of cultivation in order to identify some of the proteins involved in the biofilm phenotype. A proteomic analysis of sessile or planktonic bacteria of the same age was carried out by two-dimensional electrophoresis, matrix-assist...
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| Veröffentlicht in: | FEMS microbiology letters 2002-09, Vol.215 (1), p.7-14 |
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| creator | Trémoulet, Frédéric Duché, Ophélie Namane, Abdelkader Martinie, Brigitte Labadie, Jean-Claude |
| description | Abstract
Escherichia coli 0157:H7 biofilms were studied by a new method of cultivation in order to identify some of the proteins involved in the biofilm phenotype. A proteomic analysis of sessile or planktonic bacteria of the same age was carried out by two-dimensional electrophoresis, matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) and database searching. Comparison of two-dimensional gels showed clear differences between protein patterns of sessile and planktonic cells. Fourteen proteins increased in biofilms, whereas three decreased. From these 17 proteins, 10 were identified by MALDI-TOF-MS and could be classified into four categories according to their function: (1) general metabolism proteins (malate dehydrogenase, thiamine-phosphate pyrophosphorylase), (2) sugar and amino acid transporters (d-ribose-binding periplasmic protein, d-galactose-binding protein, YBEJ), (3) regulator proteins (DNA starvation protein and H-NS) and (4) three proteins with unknown function. The results of this study showed that E. coli O157:H7 modified the expression of several proteins involved in biofilm growth mode. |
| doi_str_mv | 10.1111/j.1574-6968.2002.tb11363.x |
| format | Article |
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Escherichia coli 0157:H7 biofilms were studied by a new method of cultivation in order to identify some of the proteins involved in the biofilm phenotype. A proteomic analysis of sessile or planktonic bacteria of the same age was carried out by two-dimensional electrophoresis, matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) and database searching. Comparison of two-dimensional gels showed clear differences between protein patterns of sessile and planktonic cells. Fourteen proteins increased in biofilms, whereas three decreased. From these 17 proteins, 10 were identified by MALDI-TOF-MS and could be classified into four categories according to their function: (1) general metabolism proteins (malate dehydrogenase, thiamine-phosphate pyrophosphorylase), (2) sugar and amino acid transporters (d-ribose-binding periplasmic protein, d-galactose-binding protein, YBEJ), (3) regulator proteins (DNA starvation protein and H-NS) and (4) three proteins with unknown function. The results of this study showed that E. coli O157:H7 modified the expression of several proteins involved in biofilm growth mode.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2002.tb11363.x</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino acids ; Bacteria ; Biofilm ; Biofilms ; Cultivation ; D-Galactose ; D-Ribose ; Database searching ; E coli ; Electrophoresis ; Escherichia coli ; Escherichia coli O157 H7 ; Galactose ; Gels ; Ionization ; Ions ; Malate dehydrogenase ; Mass spectrometry ; Mass spectroscopy ; Matrix‐assisted laser desorption ionization‐time of flight ; Microbiology ; Phenotypes ; Planktonic cells ; Protein transport ; Proteins ; Proteome ; Ribose ; Sessile species ; Thiamine ; Two‐dimensionnal electrophoresis</subject><ispartof>FEMS microbiology letters, 2002-09, Vol.215 (1), p.7-14</ispartof><rights>2002 Federation of European Microbiological Societies 2002</rights><rights>2002 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2357-c33005c4169601c7f6de80d45f55bef3b9686f1f28bb67e1ffdee24ccbc63c613</citedby><cites>FETCH-LOGICAL-c2357-c33005c4169601c7f6de80d45f55bef3b9686f1f28bb67e1ffdee24ccbc63c613</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.1574-6968.2002.tb11363.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2002.tb11363.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27922,27923,45572,45573</link.rule.ids></links><search><creatorcontrib>Trémoulet, Frédéric</creatorcontrib><creatorcontrib>Duché, Ophélie</creatorcontrib><creatorcontrib>Namane, Abdelkader</creatorcontrib><creatorcontrib>Martinie, Brigitte</creatorcontrib><creatorcontrib>Labadie, Jean-Claude</creatorcontrib><title>A proteomic study of Escherichia coli O157:H7 NCTC 12900 cultivated in biofilm or in planktonic growth mode</title><title>FEMS microbiology letters</title><description>Abstract
Escherichia coli 0157:H7 biofilms were studied by a new method of cultivation in order to identify some of the proteins involved in the biofilm phenotype. A proteomic analysis of sessile or planktonic bacteria of the same age was carried out by two-dimensional electrophoresis, matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) and database searching. Comparison of two-dimensional gels showed clear differences between protein patterns of sessile and planktonic cells. Fourteen proteins increased in biofilms, whereas three decreased. From these 17 proteins, 10 were identified by MALDI-TOF-MS and could be classified into four categories according to their function: (1) general metabolism proteins (malate dehydrogenase, thiamine-phosphate pyrophosphorylase), (2) sugar and amino acid transporters (d-ribose-binding periplasmic protein, d-galactose-binding protein, YBEJ), (3) regulator proteins (DNA starvation protein and H-NS) and (4) three proteins with unknown function. The results of this study showed that E. coli O157:H7 modified the expression of several proteins involved in biofilm growth mode.</description><subject>Amino acids</subject><subject>Bacteria</subject><subject>Biofilm</subject><subject>Biofilms</subject><subject>Cultivation</subject><subject>D-Galactose</subject><subject>D-Ribose</subject><subject>Database searching</subject><subject>E coli</subject><subject>Electrophoresis</subject><subject>Escherichia coli</subject><subject>Escherichia coli O157 H7</subject><subject>Galactose</subject><subject>Gels</subject><subject>Ionization</subject><subject>Ions</subject><subject>Malate dehydrogenase</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Matrix‐assisted laser desorption ionization‐time of flight</subject><subject>Microbiology</subject><subject>Phenotypes</subject><subject>Planktonic cells</subject><subject>Protein transport</subject><subject>Proteins</subject><subject>Proteome</subject><subject>Ribose</subject><subject>Sessile species</subject><subject>Thiamine</subject><subject>Two‐dimensionnal electrophoresis</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVkEFPwjAUxxujiYh-h0bPm6_r1g7ihRAQE5QLnputa6UwKHabwLe3y4gnPdhL0_T9_u-9H0L3BELiz-M6JAmPAzZgaRgBRGGdE0IZDY8XqPfzdYl6QHkaEBjwa3RTVWsAiCNgPbQZ4b2ztbJbI3FVN8UJW40nlVwpZ-TKZFja0uCFzxrOOH4bL8eYRAMALJuyNl9ZrQpsdjg3Vptyi61rX_sy221qu_OZH84e6hXe2kLdoiudlZW6O9999D6dLMezYL54fhmP5oGMaMIDSSlAImPiRwciuWaFSqGIE50kudI09xsxTXSU5jnjimhdKBXFUuaSUckI7aOHLtdv9tmoqhZr27idbykiSoCxhPHUVw27KulsVTmlxd6ZbeZOgoBo5Yq1aA2K1qBo5YqzXHH08FMHH0ypTv8gxfR1zj2edLht9n_AwW9tvwFahY-t</recordid><startdate>20020901</startdate><enddate>20020901</enddate><creator>Trémoulet, Frédéric</creator><creator>Duché, Ophélie</creator><creator>Namane, Abdelkader</creator><creator>Martinie, Brigitte</creator><creator>Labadie, Jean-Claude</creator><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><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>AEUYN</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>RC3</scope></search><sort><creationdate>20020901</creationdate><title>A proteomic study of Escherichia coli O157:H7 NCTC 12900 cultivated in biofilm or in planktonic growth mode</title><author>Trémoulet, Frédéric ; Duché, Ophélie ; Namane, Abdelkader ; Martinie, Brigitte ; Labadie, Jean-Claude</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2357-c33005c4169601c7f6de80d45f55bef3b9686f1f28bb67e1ffdee24ccbc63c613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino acids</topic><topic>Bacteria</topic><topic>Biofilm</topic><topic>Biofilms</topic><topic>Cultivation</topic><topic>D-Galactose</topic><topic>D-Ribose</topic><topic>Database searching</topic><topic>E coli</topic><topic>Electrophoresis</topic><topic>Escherichia coli</topic><topic>Escherichia coli O157 H7</topic><topic>Galactose</topic><topic>Gels</topic><topic>Ionization</topic><topic>Ions</topic><topic>Malate dehydrogenase</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Matrix‐assisted laser desorption ionization‐time of flight</topic><topic>Microbiology</topic><topic>Phenotypes</topic><topic>Planktonic cells</topic><topic>Protein transport</topic><topic>Proteins</topic><topic>Proteome</topic><topic>Ribose</topic><topic>Sessile species</topic><topic>Thiamine</topic><topic>Two‐dimensionnal electrophoresis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Trémoulet, Frédéric</creatorcontrib><creatorcontrib>Duché, Ophélie</creatorcontrib><creatorcontrib>Namane, Abdelkader</creatorcontrib><creatorcontrib>Martinie, Brigitte</creatorcontrib><creatorcontrib>Labadie, Jean-Claude</creatorcontrib><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 Edition)</collection><collection>ProQuest One Sustainability</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 (ProQuest)</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>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</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>Genetics Abstracts</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Trémoulet, Frédéric</au><au>Duché, Ophélie</au><au>Namane, Abdelkader</au><au>Martinie, Brigitte</au><au>Labadie, Jean-Claude</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A proteomic study of Escherichia coli O157:H7 NCTC 12900 cultivated in biofilm or in planktonic growth mode</atitle><jtitle>FEMS microbiology letters</jtitle><date>2002-09-01</date><risdate>2002</risdate><volume>215</volume><issue>1</issue><spage>7</spage><epage>14</epage><pages>7-14</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><abstract>Abstract
Escherichia coli 0157:H7 biofilms were studied by a new method of cultivation in order to identify some of the proteins involved in the biofilm phenotype. A proteomic analysis of sessile or planktonic bacteria of the same age was carried out by two-dimensional electrophoresis, matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) and database searching. Comparison of two-dimensional gels showed clear differences between protein patterns of sessile and planktonic cells. Fourteen proteins increased in biofilms, whereas three decreased. From these 17 proteins, 10 were identified by MALDI-TOF-MS and could be classified into four categories according to their function: (1) general metabolism proteins (malate dehydrogenase, thiamine-phosphate pyrophosphorylase), (2) sugar and amino acid transporters (d-ribose-binding periplasmic protein, d-galactose-binding protein, YBEJ), (3) regulator proteins (DNA starvation protein and H-NS) and (4) three proteins with unknown function. The results of this study showed that E. coli O157:H7 modified the expression of several proteins involved in biofilm growth mode.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/j.1574-6968.2002.tb11363.x</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2002-09, Vol.215 (1), p.7-14 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_journals_2310665678 |
| source | Wiley Online Library Journals Frontfile Complete; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Amino acids Bacteria Biofilm Biofilms Cultivation D-Galactose D-Ribose Database searching E coli Electrophoresis Escherichia coli Escherichia coli O157 H7 Galactose Gels Ionization Ions Malate dehydrogenase Mass spectrometry Mass spectroscopy Matrix‐assisted laser desorption ionization‐time of flight Microbiology Phenotypes Planktonic cells Protein transport Proteins Proteome Ribose Sessile species Thiamine Two‐dimensionnal electrophoresis |
| title | A proteomic study of Escherichia coli O157:H7 NCTC 12900 cultivated in biofilm or in planktonic growth mode |
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