Loading…
Heterologous extracellular production of enterocin P from Enterococcus faecium P13 in the methylotrophic bacterium Methylobacterium extorquens
Enterocin P (EntP), a strong antilisterial pediocin-like bacteriocin from Enterococcus faecium P13, was produced by Methylobacterium extorquens. For heterologous expression of EntP in the methylotrophic bacterium M. extorquens, a recombinant plasmid was constructed. The gene encoding the EntP struct...
Saved in:
| Published in: | FEMS microbiology letters 2005-07, Vol.248 (1), p.125-131 |
|---|---|
| Main Authors: | , , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | |
|---|---|
| cites | cdi_FETCH-LOGICAL-c5515-754a74519a2659237c7ddadebfff2ec501ddfdb19ba7270d1c8b87f5f921a7b93 |
| container_end_page | 131 |
| container_issue | 1 |
| container_start_page | 125 |
| container_title | FEMS microbiology letters |
| container_volume | 248 |
| creator | Gutiérrez, Jorge Bourque, Denis Criado, Raquel Choi, Young J. Cintas, Luis M. Hernández, Pablo E. Míguez, Carlos B. |
| description | Enterocin P (EntP), a strong antilisterial pediocin-like bacteriocin from
Enterococcus faecium P13, was produced by
Methylobacterium extorquens. For heterologous expression of EntP in the methylotrophic bacterium
M. extorquens, a recombinant plasmid was constructed. The gene encoding the EntP structural gene (
entP) was cloned into the plasmid vector pCM80, under control of the methanol dehydrogenase promoter (P
mxaF), to generate plasmid pS25. When
M. extorquens ATCC 55366 was transformed with pS25, EntP was detected and quantified in supernatants of the recombinant
M. extorquens S25 strain by using specific anti-EntP antibodies and a non-competitive indirect enzyme-linked immunosorbent assay (NCI-ELISA). Purification of EntP by hydrophobic adsorption and reverse-phase (RP-FPLC) chromatographies, permitted recovery of active EntP from the supernatants of
M. extorquens S25 grown in a synthetic defined medium. |
| doi_str_mv | 10.1016/j.femsle.2005.05.029 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67954959</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><oup_id>10.1016/j.femsle.2005.05.029</oup_id><els_id>S0378109705003216</els_id><sourcerecordid>2306554931</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5515-754a74519a2659237c7ddadebfff2ec501ddfdb19ba7270d1c8b87f5f921a7b93</originalsourceid><addsrcrecordid>eNqNkdFqFDEUhoModq2-gUhA9G62SWYymdwIpbRW2GIv9DpkkhM3y8xkTWbUfYk-czPMwoIXWjgQSL7_P-fkR-gtJWtKaH2xWzvoUwdrRghfz8XkM7SiXFRFLevmOVqRUjQFJVKcoVcp7QghFSP1S3RGueSkImyFHm5hhBi68CNMCcOfMWoDXTd1OuJ9DHYyow8DDg7DMIPGD_geuxh6fL1cBGOy0mkwfurxPS1xRsYt4B7G7aELYwz7rTe41SbzM3O3PJwuctsQf04wpNfohdNdgjfH8xx9v7n-dnVbbL5-_nJ1uSkM55QXgldaVJxKzWouWSmMsFZbaJ1zDAwn1FpnWypbLZgglpqmbYTjTjKqRSvLc_Rx8c075sZpVL1P8-J6gPwRqhaSV5L_H6SikoLzJoPv_wJ3YYpDXkKxktQ825U0U9VCmRhSiuDUPvpex4OiRM2xqp1aYlVzrGouNk_x7mg-tT3Yk-iYYwY-HAGdjO5c1IPx6cTVTVPRcuaahfvtOzg8qbm6udtQxrP0YpGGaf_UqT8tCshJ_vIQVTIeBgPWRzCjssH_2-ARKxPm-A</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2306554931</pqid></control><display><type>article</type><title>Heterologous extracellular production of enterocin P from Enterococcus faecium P13 in the methylotrophic bacterium Methylobacterium extorquens</title><source>Oxford Journals Online</source><creator>Gutiérrez, Jorge ; Bourque, Denis ; Criado, Raquel ; Choi, Young J. ; Cintas, Luis M. ; Hernández, Pablo E. ; Míguez, Carlos B.</creator><creatorcontrib>Gutiérrez, Jorge ; Bourque, Denis ; Criado, Raquel ; Choi, Young J. ; Cintas, Luis M. ; Hernández, Pablo E. ; Míguez, Carlos B.</creatorcontrib><description>Enterocin P (EntP), a strong antilisterial pediocin-like bacteriocin from
Enterococcus faecium P13, was produced by
Methylobacterium extorquens. For heterologous expression of EntP in the methylotrophic bacterium
M. extorquens, a recombinant plasmid was constructed. The gene encoding the EntP structural gene (
entP) was cloned into the plasmid vector pCM80, under control of the methanol dehydrogenase promoter (P
mxaF), to generate plasmid pS25. When
M. extorquens ATCC 55366 was transformed with pS25, EntP was detected and quantified in supernatants of the recombinant
M. extorquens S25 strain by using specific anti-EntP antibodies and a non-competitive indirect enzyme-linked immunosorbent assay (NCI-ELISA). Purification of EntP by hydrophobic adsorption and reverse-phase (RP-FPLC) chromatographies, permitted recovery of active EntP from the supernatants of
M. extorquens S25 grown in a synthetic defined medium.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1016/j.femsle.2005.05.029</identifier><identifier>PMID: 15950402</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Elsevier B.V</publisher><subject>Antibodies ; Bacteria ; Bacteriocins ; Bacteriocins - biosynthesis ; Bacteriocins - genetics ; Bacteriology ; Biological and medical sciences ; Enterocin P ; Enterococcus faecium ; Enterococcus faecium - genetics ; Enterococcus faecium - metabolism ; Enzyme-linked immunosorbent assay ; Fundamental and applied biological sciences. Psychology ; General secretory pathway ; Genetics ; Heterologous gene expression ; Hydrophobicity ; Liquid chromatography ; Methanol dehydrogenase ; Methylobacterium extorquens ; Methylobacterium extorquens - genetics ; Methylobacterium extorquens - growth & development ; Methylobacterium extorquens - metabolism ; Microbiology ; Pediocin ; Plasmids ; Purification ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - isolation & purification</subject><ispartof>FEMS microbiology letters, 2005-07, Vol.248 (1), p.125-131</ispartof><rights>2005 Federation of European Microbiological Societies</rights><rights>2005 Federation of European Microbiological Societies 2005</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c5515-754a74519a2659237c7ddadebfff2ec501ddfdb19ba7270d1c8b87f5f921a7b93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16884132$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15950402$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gutiérrez, Jorge</creatorcontrib><creatorcontrib>Bourque, Denis</creatorcontrib><creatorcontrib>Criado, Raquel</creatorcontrib><creatorcontrib>Choi, Young J.</creatorcontrib><creatorcontrib>Cintas, Luis M.</creatorcontrib><creatorcontrib>Hernández, Pablo E.</creatorcontrib><creatorcontrib>Míguez, Carlos B.</creatorcontrib><title>Heterologous extracellular production of enterocin P from Enterococcus faecium P13 in the methylotrophic bacterium Methylobacterium extorquens</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Enterocin P (EntP), a strong antilisterial pediocin-like bacteriocin from
Enterococcus faecium P13, was produced by
Methylobacterium extorquens. For heterologous expression of EntP in the methylotrophic bacterium
M. extorquens, a recombinant plasmid was constructed. The gene encoding the EntP structural gene (
entP) was cloned into the plasmid vector pCM80, under control of the methanol dehydrogenase promoter (P
mxaF), to generate plasmid pS25. When
M. extorquens ATCC 55366 was transformed with pS25, EntP was detected and quantified in supernatants of the recombinant
M. extorquens S25 strain by using specific anti-EntP antibodies and a non-competitive indirect enzyme-linked immunosorbent assay (NCI-ELISA). Purification of EntP by hydrophobic adsorption and reverse-phase (RP-FPLC) chromatographies, permitted recovery of active EntP from the supernatants of
M. extorquens S25 grown in a synthetic defined medium.</description><subject>Antibodies</subject><subject>Bacteria</subject><subject>Bacteriocins</subject><subject>Bacteriocins - biosynthesis</subject><subject>Bacteriocins - genetics</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Enterocin P</subject><subject>Enterococcus faecium</subject><subject>Enterococcus faecium - genetics</subject><subject>Enterococcus faecium - metabolism</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General secretory pathway</subject><subject>Genetics</subject><subject>Heterologous gene expression</subject><subject>Hydrophobicity</subject><subject>Liquid chromatography</subject><subject>Methanol dehydrogenase</subject><subject>Methylobacterium extorquens</subject><subject>Methylobacterium extorquens - genetics</subject><subject>Methylobacterium extorquens - growth & development</subject><subject>Methylobacterium extorquens - metabolism</subject><subject>Microbiology</subject><subject>Pediocin</subject><subject>Plasmids</subject><subject>Purification</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - isolation & purification</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqNkdFqFDEUhoModq2-gUhA9G62SWYymdwIpbRW2GIv9DpkkhM3y8xkTWbUfYk-czPMwoIXWjgQSL7_P-fkR-gtJWtKaH2xWzvoUwdrRghfz8XkM7SiXFRFLevmOVqRUjQFJVKcoVcp7QghFSP1S3RGueSkImyFHm5hhBi68CNMCcOfMWoDXTd1OuJ9DHYyow8DDg7DMIPGD_geuxh6fL1cBGOy0mkwfurxPS1xRsYt4B7G7aELYwz7rTe41SbzM3O3PJwuctsQf04wpNfohdNdgjfH8xx9v7n-dnVbbL5-_nJ1uSkM55QXgldaVJxKzWouWSmMsFZbaJ1zDAwn1FpnWypbLZgglpqmbYTjTjKqRSvLc_Rx8c075sZpVL1P8-J6gPwRqhaSV5L_H6SikoLzJoPv_wJ3YYpDXkKxktQ825U0U9VCmRhSiuDUPvpex4OiRM2xqp1aYlVzrGouNk_x7mg-tT3Yk-iYYwY-HAGdjO5c1IPx6cTVTVPRcuaahfvtOzg8qbm6udtQxrP0YpGGaf_UqT8tCshJ_vIQVTIeBgPWRzCjssH_2-ARKxPm-A</recordid><startdate>200507</startdate><enddate>200507</enddate><creator>Gutiérrez, Jorge</creator><creator>Bourque, Denis</creator><creator>Criado, Raquel</creator><creator>Choi, Young J.</creator><creator>Cintas, Luis M.</creator><creator>Hernández, Pablo E.</creator><creator>Míguez, Carlos B.</creator><general>Elsevier B.V</general><general>Blackwell Publishing Ltd</general><general>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>RC3</scope><scope>7X8</scope></search><sort><creationdate>200507</creationdate><title>Heterologous extracellular production of enterocin P from Enterococcus faecium P13 in the methylotrophic bacterium Methylobacterium extorquens</title><author>Gutiérrez, Jorge ; Bourque, Denis ; Criado, Raquel ; Choi, Young J. ; Cintas, Luis M. ; Hernández, Pablo E. ; Míguez, Carlos B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5515-754a74519a2659237c7ddadebfff2ec501ddfdb19ba7270d1c8b87f5f921a7b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Antibodies</topic><topic>Bacteria</topic><topic>Bacteriocins</topic><topic>Bacteriocins - biosynthesis</topic><topic>Bacteriocins - genetics</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Enterocin P</topic><topic>Enterococcus faecium</topic><topic>Enterococcus faecium - genetics</topic><topic>Enterococcus faecium - metabolism</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General secretory pathway</topic><topic>Genetics</topic><topic>Heterologous gene expression</topic><topic>Hydrophobicity</topic><topic>Liquid chromatography</topic><topic>Methanol dehydrogenase</topic><topic>Methylobacterium extorquens</topic><topic>Methylobacterium extorquens - genetics</topic><topic>Methylobacterium extorquens - growth & development</topic><topic>Methylobacterium extorquens - metabolism</topic><topic>Microbiology</topic><topic>Pediocin</topic><topic>Plasmids</topic><topic>Purification</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gutiérrez, Jorge</creatorcontrib><creatorcontrib>Bourque, Denis</creatorcontrib><creatorcontrib>Criado, Raquel</creatorcontrib><creatorcontrib>Choi, Young J.</creatorcontrib><creatorcontrib>Cintas, Luis M.</creatorcontrib><creatorcontrib>Hernández, Pablo E.</creatorcontrib><creatorcontrib>Míguez, Carlos B.</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>ProQuest 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 (Proquest) (PQ_SDU_P3)</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><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gutiérrez, Jorge</au><au>Bourque, Denis</au><au>Criado, Raquel</au><au>Choi, Young J.</au><au>Cintas, Luis M.</au><au>Hernández, Pablo E.</au><au>Míguez, Carlos B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heterologous extracellular production of enterocin P from Enterococcus faecium P13 in the methylotrophic bacterium Methylobacterium extorquens</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2005-07</date><risdate>2005</risdate><volume>248</volume><issue>1</issue><spage>125</spage><epage>131</epage><pages>125-131</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Enterocin P (EntP), a strong antilisterial pediocin-like bacteriocin from
Enterococcus faecium P13, was produced by
Methylobacterium extorquens. For heterologous expression of EntP in the methylotrophic bacterium
M. extorquens, a recombinant plasmid was constructed. The gene encoding the EntP structural gene (
entP) was cloned into the plasmid vector pCM80, under control of the methanol dehydrogenase promoter (P
mxaF), to generate plasmid pS25. When
M. extorquens ATCC 55366 was transformed with pS25, EntP was detected and quantified in supernatants of the recombinant
M. extorquens S25 strain by using specific anti-EntP antibodies and a non-competitive indirect enzyme-linked immunosorbent assay (NCI-ELISA). Purification of EntP by hydrophobic adsorption and reverse-phase (RP-FPLC) chromatographies, permitted recovery of active EntP from the supernatants of
M. extorquens S25 grown in a synthetic defined medium.</abstract><cop>Oxford, UK</cop><pub>Elsevier B.V</pub><pmid>15950402</pmid><doi>10.1016/j.femsle.2005.05.029</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2005-07, Vol.248 (1), p.125-131 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67954959 |
| source | Oxford Journals Online |
| subjects | Antibodies Bacteria Bacteriocins Bacteriocins - biosynthesis Bacteriocins - genetics Bacteriology Biological and medical sciences Enterocin P Enterococcus faecium Enterococcus faecium - genetics Enterococcus faecium - metabolism Enzyme-linked immunosorbent assay Fundamental and applied biological sciences. Psychology General secretory pathway Genetics Heterologous gene expression Hydrophobicity Liquid chromatography Methanol dehydrogenase Methylobacterium extorquens Methylobacterium extorquens - genetics Methylobacterium extorquens - growth & development Methylobacterium extorquens - metabolism Microbiology Pediocin Plasmids Purification Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification |
| title | Heterologous extracellular production of enterocin P from Enterococcus faecium P13 in the methylotrophic bacterium Methylobacterium extorquens |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T17%3A41%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Heterologous%20extracellular%20production%20of%20enterocin%20P%20from%20Enterococcus%20faecium%20P13%20in%20the%20methylotrophic%20bacterium%20Methylobacterium%20extorquens&rft.jtitle=FEMS%20microbiology%20letters&rft.au=Guti%C3%A9rrez,%20Jorge&rft.date=2005-07&rft.volume=248&rft.issue=1&rft.spage=125&rft.epage=131&rft.pages=125-131&rft.issn=0378-1097&rft.eissn=1574-6968&rft.coden=FMLED7&rft_id=info:doi/10.1016/j.femsle.2005.05.029&rft_dat=%3Cproquest_cross%3E2306554931%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c5515-754a74519a2659237c7ddadebfff2ec501ddfdb19ba7270d1c8b87f5f921a7b93%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2306554931&rft_id=info:pmid/15950402&rft_oup_id=10.1016/j.femsle.2005.05.029&rfr_iscdi=true |