Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity
A collection of pediocin AcH amino acid substitution mutants was generated by PCR random mutagenesis of DNA encoding the bacteriocin. Mutants were isolated by cloning mutagenized DNA into an Escherichia coli malE plasmid that directs the secretion of maltose binding protein-pediocin AcH chimeric pro...
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| Veröffentlicht in: | Applied and Environmental Microbiology 1998-06, Vol.64 (6), p.1997-2005 |
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| creator | Miller, K.W. (University of Wyoming, Laramie, WY.) Schamber, R Osmanagaoglu, O Ray, B |
| description | A collection of pediocin AcH amino acid substitution mutants was generated by PCR random mutagenesis of DNA encoding the bacteriocin. Mutants were isolated by cloning mutagenized DNA into an Escherichia coli malE plasmid that directs the secretion of maltose binding protein-pediocin AcH chimeric proteins and by screening transformant colonies for bactericidal activity against Lactobacillus plantarum NCDO955 (K. W. Miller, R. Schamber, Y. Chen, and B. Ray, 1998. Appl. Environ. Microbiol. 64:14-20, 1998). In all, 17 substitution mutants were isolated at 14 of the 44 amino acids of pediocin AcH. Seven mutants (N5K, C9R, C14S, C14Y, G37E, G37R, and C44W) were completely inactive against the pediocin AcH-sensitive strains L. plantarum NCDO955, Listeria innocua Lin11, Enterococcus faecalis M1, Pediococcus acidilactici LB42, and Leuconostoc mesenteroides Ly. A C24S substitution mutant constructed by other means also was inactive against these bacteria. Nine other mutants (K1N, W18R, I26T, M31T, A34D, N41K, H42L, K43N, and K43E) retained from 1% to approximately 60% of wild-type activity when assayed against L. innocua Lin11. One mutant, K11E, displayed approximately 2.8-fold-higher activity against this indicator. About one half of the mutations mapped to amino acids that are conserved in the pediocin-like family of bacteriocins. All four cysteines were found to be required for activity, although only C9 and C14 are conserved among pediocin-like bacteriocins. Several basic amino acids as well as nonpolar amino acids located within the hydrophobic C-terminal region also were found to be important. The mutations are discussed in the context of structural models that have been proposed for the bacteriocin |
| doi_str_mv | 10.1128/aem.64.6.1997-2005.1998 |
| format | Article |
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(University of Wyoming, Laramie, WY.) ; Schamber, R ; Osmanagaoglu, O ; Ray, B</creator><creatorcontrib>Miller, K.W. (University of Wyoming, Laramie, WY.) ; Schamber, R ; Osmanagaoglu, O ; Ray, B</creatorcontrib><description>A collection of pediocin AcH amino acid substitution mutants was generated by PCR random mutagenesis of DNA encoding the bacteriocin. Mutants were isolated by cloning mutagenized DNA into an Escherichia coli malE plasmid that directs the secretion of maltose binding protein-pediocin AcH chimeric proteins and by screening transformant colonies for bactericidal activity against Lactobacillus plantarum NCDO955 (K. W. Miller, R. Schamber, Y. Chen, and B. Ray, 1998. Appl. Environ. Microbiol. 64:14-20, 1998). In all, 17 substitution mutants were isolated at 14 of the 44 amino acids of pediocin AcH. Seven mutants (N5K, C9R, C14S, C14Y, G37E, G37R, and C44W) were completely inactive against the pediocin AcH-sensitive strains L. plantarum NCDO955, Listeria innocua Lin11, Enterococcus faecalis M1, Pediococcus acidilactici LB42, and Leuconostoc mesenteroides Ly. A C24S substitution mutant constructed by other means also was inactive against these bacteria. Nine other mutants (K1N, W18R, I26T, M31T, A34D, N41K, H42L, K43N, and K43E) retained from 1% to approximately 60% of wild-type activity when assayed against L. innocua Lin11. One mutant, K11E, displayed approximately 2.8-fold-higher activity against this indicator. About one half of the mutations mapped to amino acids that are conserved in the pediocin-like family of bacteriocins. All four cysteines were found to be required for activity, although only C9 and C14 are conserved among pediocin-like bacteriocins. Several basic amino acids as well as nonpolar amino acids located within the hydrophobic C-terminal region also were found to be important. The mutations are discussed in the context of structural models that have been proposed for the bacteriocin</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>DOI: 10.1128/aem.64.6.1997-2005.1998</identifier><identifier>PMID: 9603806</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>ACIDE AMINE ; Amino Acid Sequence ; AMINO ACIDS ; AMINOACIDOS ; ANTIBACTERIAL PROPERTIES ; ANTIMICROBIAL PROPERTIES ; ATP-Binding Cassette Transporters ; Bacteria ; Bacteriocins - genetics ; Bacteriocins - isolation & purification ; Bacteriocins - pharmacology ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Carrier Proteins - genetics ; Carrier Proteins - isolation & purification ; Cloning, Molecular ; DNA Primers - genetics ; Enterococcus faecalis - drug effects ; Escherichia coli - genetics ; Escherichia coli Proteins ; Fundamental and applied biological sciences. Psychology ; Genetics and Molecular Biology ; Lactococcus - drug effects ; Leuconostoc - drug effects ; Listeria - drug effects ; Maltose-Binding Proteins ; Methods. Procedures. Technologies ; Microbiology ; Monosaccharide Transport Proteins ; MUTANT ; MUTANTES ; MUTANTS ; Mutation ; pediocin AcH ; Pediocins ; Pediococcus - genetics ; Periplasmic Binding Proteins ; Plasmids - genetics ; Point Mutation ; Polymerase Chain Reaction ; PROPIEDADES ANTIMICROBIANAS ; PROPRIETE ANTIMICROBIENNE ; Protein engineering ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - isolation & purification ; Recombinant Fusion Proteins - pharmacology ; Transformation, Genetic</subject><ispartof>Applied and Environmental Microbiology, 1998-06, Vol.64 (6), p.1997-2005</ispartof><rights>1998 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Jun 1998</rights><rights>Copyright © 1998, American Society for Microbiology 1998</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c546t-81adf2470061bc96c3a48f03f7a31626dca9cf7f3fbbffe52c6c531c0bd788bf3</citedby><cites>FETCH-LOGICAL-c546t-81adf2470061bc96c3a48f03f7a31626dca9cf7f3fbbffe52c6c531c0bd788bf3</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/PMC106270/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC106270/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,728,781,785,886,3189,3190,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2272919$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9603806$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Miller, K.W. (University of Wyoming, Laramie, WY.)</creatorcontrib><creatorcontrib>Schamber, R</creatorcontrib><creatorcontrib>Osmanagaoglu, O</creatorcontrib><creatorcontrib>Ray, B</creatorcontrib><title>Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>A collection of pediocin AcH amino acid substitution mutants was generated by PCR random mutagenesis of DNA encoding the bacteriocin. Mutants were isolated by cloning mutagenized DNA into an Escherichia coli malE plasmid that directs the secretion of maltose binding protein-pediocin AcH chimeric proteins and by screening transformant colonies for bactericidal activity against Lactobacillus plantarum NCDO955 (K. W. Miller, R. Schamber, Y. Chen, and B. Ray, 1998. Appl. Environ. Microbiol. 64:14-20, 1998). In all, 17 substitution mutants were isolated at 14 of the 44 amino acids of pediocin AcH. Seven mutants (N5K, C9R, C14S, C14Y, G37E, G37R, and C44W) were completely inactive against the pediocin AcH-sensitive strains L. plantarum NCDO955, Listeria innocua Lin11, Enterococcus faecalis M1, Pediococcus acidilactici LB42, and Leuconostoc mesenteroides Ly. A C24S substitution mutant constructed by other means also was inactive against these bacteria. Nine other mutants (K1N, W18R, I26T, M31T, A34D, N41K, H42L, K43N, and K43E) retained from 1% to approximately 60% of wild-type activity when assayed against L. innocua Lin11. One mutant, K11E, displayed approximately 2.8-fold-higher activity against this indicator. About one half of the mutations mapped to amino acids that are conserved in the pediocin-like family of bacteriocins. All four cysteines were found to be required for activity, although only C9 and C14 are conserved among pediocin-like bacteriocins. Several basic amino acids as well as nonpolar amino acids located within the hydrophobic C-terminal region also were found to be important. The mutations are discussed in the context of structural models that have been proposed for the bacteriocin</description><subject>ACIDE AMINE</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACIDS</subject><subject>AMINOACIDOS</subject><subject>ANTIBACTERIAL PROPERTIES</subject><subject>ANTIMICROBIAL PROPERTIES</subject><subject>ATP-Binding Cassette Transporters</subject><subject>Bacteria</subject><subject>Bacteriocins - genetics</subject><subject>Bacteriocins - isolation & purification</subject><subject>Bacteriocins - pharmacology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Cloning, Molecular</subject><subject>DNA Primers - genetics</subject><subject>Enterococcus faecalis - drug effects</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli Proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetics and Molecular Biology</subject><subject>Lactococcus - drug effects</subject><subject>Leuconostoc - drug effects</subject><subject>Listeria - drug effects</subject><subject>Maltose-Binding Proteins</subject><subject>Methods. Procedures. Technologies</subject><subject>Microbiology</subject><subject>Monosaccharide Transport Proteins</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>MUTANTS</subject><subject>Mutation</subject><subject>pediocin AcH</subject><subject>Pediocins</subject><subject>Pediococcus - genetics</subject><subject>Periplasmic Binding Proteins</subject><subject>Plasmids - genetics</subject><subject>Point Mutation</subject><subject>Polymerase Chain Reaction</subject><subject>PROPIEDADES ANTIMICROBIANAS</subject><subject>PROPRIETE ANTIMICROBIENNE</subject><subject>Protein engineering</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>Recombinant Fusion Proteins - pharmacology</subject><subject>Transformation, Genetic</subject><issn>0099-2240</issn><issn>1098-5336</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkkFv1DAQhSMEKkvhJyACQtyyjO3EsQ89rKpCKxVxgJ6tiWPvepXEi520Kr8eR1ltgZNHft-b8eg5y94RWBNCxWc0_ZqXa74mUtYFBajmSjzLVgSkKCrG-PNsBSBlQWkJL7NXMe4BoAQuzrIzyYEJ4KtsfxN9h6PzQ45Dm-sdBtSjCe73cultfjCt89oN-UZfJ8D1SdX5IfjRpMt-GnEYY_7gxl2OXbKaNm-WHtq12OWpdvdufHydvbDYRfPmeJ5nd1-ufl5eF7ffv95cbm4LXZV8LATB1tKyBuCk0ZJrhqWwwGyNjHDKW41S29oy2zTWmopqritGNDRtLURj2Xl2sfQ9TE1vWm2GMWCnDsH1GB6VR6f-VQa3U1t_rwhwWkPyfzr6g_81mTiq3kVtug4H46eoSF1xUVOewA__gXs_hSHtpihUsiwJKRNUL5AOPsZg7OkhBNQcpdpcfVO8VFzNUao5yrkSyfn27z1OvmN2Sf941DFq7GzAQbt4wiitqSQyYe8XbOe2uwcXjMLYq_R_noY-jbLoFW5DanP3Y1ZAMiCc_QF-cL7k</recordid><startdate>19980601</startdate><enddate>19980601</enddate><creator>Miller, K.W. (University of Wyoming, Laramie, WY.)</creator><creator>Schamber, R</creator><creator>Osmanagaoglu, O</creator><creator>Ray, B</creator><general>American Society for Microbiology</general><scope>FBQ</scope><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>7QO</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T7</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><scope>SOI</scope><scope>5PM</scope></search><sort><creationdate>19980601</creationdate><title>Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity</title><author>Miller, K.W. (University of Wyoming, Laramie, WY.) ; Schamber, R ; Osmanagaoglu, O ; Ray, B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c546t-81adf2470061bc96c3a48f03f7a31626dca9cf7f3fbbffe52c6c531c0bd788bf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>ACIDE AMINE</topic><topic>Amino Acid Sequence</topic><topic>AMINO ACIDS</topic><topic>AMINOACIDOS</topic><topic>ANTIBACTERIAL PROPERTIES</topic><topic>ANTIMICROBIAL PROPERTIES</topic><topic>ATP-Binding Cassette Transporters</topic><topic>Bacteria</topic><topic>Bacteriocins - genetics</topic><topic>Bacteriocins - isolation & purification</topic><topic>Bacteriocins - pharmacology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Cloning, Molecular</topic><topic>DNA Primers - genetics</topic><topic>Enterococcus faecalis - drug effects</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli Proteins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetics and Molecular Biology</topic><topic>Lactococcus - drug effects</topic><topic>Leuconostoc - drug effects</topic><topic>Listeria - drug effects</topic><topic>Maltose-Binding Proteins</topic><topic>Methods. Procedures. Technologies</topic><topic>Microbiology</topic><topic>Monosaccharide Transport Proteins</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>MUTANTS</topic><topic>Mutation</topic><topic>pediocin AcH</topic><topic>Pediocins</topic><topic>Pediococcus - genetics</topic><topic>Periplasmic Binding Proteins</topic><topic>Plasmids - genetics</topic><topic>Point Mutation</topic><topic>Polymerase Chain Reaction</topic><topic>PROPIEDADES ANTIMICROBIANAS</topic><topic>PROPRIETE ANTIMICROBIENNE</topic><topic>Protein engineering</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>Recombinant Fusion Proteins - pharmacology</topic><topic>Transformation, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miller, K.W. (University of Wyoming, Laramie, WY.)</creatorcontrib><creatorcontrib>Schamber, R</creatorcontrib><creatorcontrib>Osmanagaoglu, O</creatorcontrib><creatorcontrib>Ray, B</creatorcontrib><collection>AGRIS</collection><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>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</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><collection>Environment Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied and Environmental Microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miller, K.W. (University of Wyoming, Laramie, WY.)</au><au>Schamber, R</au><au>Osmanagaoglu, O</au><au>Ray, B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>1998-06-01</date><risdate>1998</risdate><volume>64</volume><issue>6</issue><spage>1997</spage><epage>2005</epage><pages>1997-2005</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><coden>AEMIDF</coden><abstract>A collection of pediocin AcH amino acid substitution mutants was generated by PCR random mutagenesis of DNA encoding the bacteriocin. Mutants were isolated by cloning mutagenized DNA into an Escherichia coli malE plasmid that directs the secretion of maltose binding protein-pediocin AcH chimeric proteins and by screening transformant colonies for bactericidal activity against Lactobacillus plantarum NCDO955 (K. W. Miller, R. Schamber, Y. Chen, and B. Ray, 1998. Appl. Environ. Microbiol. 64:14-20, 1998). In all, 17 substitution mutants were isolated at 14 of the 44 amino acids of pediocin AcH. Seven mutants (N5K, C9R, C14S, C14Y, G37E, G37R, and C44W) were completely inactive against the pediocin AcH-sensitive strains L. plantarum NCDO955, Listeria innocua Lin11, Enterococcus faecalis M1, Pediococcus acidilactici LB42, and Leuconostoc mesenteroides Ly. A C24S substitution mutant constructed by other means also was inactive against these bacteria. Nine other mutants (K1N, W18R, I26T, M31T, A34D, N41K, H42L, K43N, and K43E) retained from 1% to approximately 60% of wild-type activity when assayed against L. innocua Lin11. One mutant, K11E, displayed approximately 2.8-fold-higher activity against this indicator. About one half of the mutations mapped to amino acids that are conserved in the pediocin-like family of bacteriocins. All four cysteines were found to be required for activity, although only C9 and C14 are conserved among pediocin-like bacteriocins. Several basic amino acids as well as nonpolar amino acids located within the hydrophobic C-terminal region also were found to be important. The mutations are discussed in the context of structural models that have been proposed for the bacteriocin</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>9603806</pmid><doi>10.1128/aem.64.6.1997-2005.1998</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Applied and Environmental Microbiology, 1998-06, Vol.64 (6), p.1997-2005 |
| issn | 0099-2240 1098-5336 |
| language | eng |
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| source | American Society for Microbiology; MEDLINE; PubMed Central; Alma/SFX Local Collection |
| subjects | ACIDE AMINE Amino Acid Sequence AMINO ACIDS AMINOACIDOS ANTIBACTERIAL PROPERTIES ANTIMICROBIAL PROPERTIES ATP-Binding Cassette Transporters Bacteria Bacteriocins - genetics Bacteriocins - isolation & purification Bacteriocins - pharmacology Base Sequence Biological and medical sciences Biotechnology Carrier Proteins - genetics Carrier Proteins - isolation & purification Cloning, Molecular DNA Primers - genetics Enterococcus faecalis - drug effects Escherichia coli - genetics Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Genetics and Molecular Biology Lactococcus - drug effects Leuconostoc - drug effects Listeria - drug effects Maltose-Binding Proteins Methods. Procedures. Technologies Microbiology Monosaccharide Transport Proteins MUTANT MUTANTES MUTANTS Mutation pediocin AcH Pediocins Pediococcus - genetics Periplasmic Binding Proteins Plasmids - genetics Point Mutation Polymerase Chain Reaction PROPIEDADES ANTIMICROBIANAS PROPRIETE ANTIMICROBIENNE Protein engineering Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - pharmacology Transformation, Genetic |
| title | Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity |
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