Expression of the antimicrobial peptide carnobacteriocin B2 by a signal peptide-dependent general secretory pathway
Carnobacteriocin B2 is a well-characterized class II bacteriocin produced by a 61-kb plasmid from Carnobacterium piscicola LV17. Export of this bacteriocin is dependent on specific ABC (ATP-binding cassette) secretion proteins. Divergicin A is a strongly hydrophobic narrow-spectrum bacteriocin produ...
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| Veröffentlicht in: | Applied and Environmental Microbiology 1996-11, Vol.62 (11), p.4095-4099 |
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| creator | McCormick, J.K. (University of Alberta, Edmonton, Alberta, Canada.) Worobo, R.W Stiles, M.E |
| description | Carnobacteriocin B2 is a well-characterized class II bacteriocin produced by a 61-kb plasmid from Carnobacterium piscicola LV17. Export of this bacteriocin is dependent on specific ABC (ATP-binding cassette) secretion proteins. Divergicin A is a strongly hydrophobic narrow-spectrum bacteriocin produced by a 3.4kb plasmid from Carnobacterium divergens LV13. Predivergicin A contains a signal peptide and utilizes the general secretary pathway for export (R.W. Worobo, M. J. van Belkum, M. Sailer, K.L. Roy, J. C. Vederas, and M. E. Stiles, J. Bacteriol. 177: 3143-3149, 1995). Fusion of the carnobacteriocin B2 structural gene (devoid of its natural leader peptide) behind the signal peptide of divergicin A in the expression vector pMG36e permitted production and export of active carnobacteriocin B2 in the absence of the specific secretion genes. N-terminal sequencing of purified carnobacteriocin B2 established that correct processing of the prebacteriocin occurred beyond the Ala-Ser-Ala cleavage site of the signal peptide. Carnobacteriocin B2 was produced by the wild-type strain of C divergens, LV13, and in C. piscicola LV17C, the nonbacteriocinogenic, plasmidless variant of the original carnobacteriocin B2 producer strain. The corresponding immunity gene was included immediately downstream of the structural gene. Both of the host strains are sensitive to the bacteriocin, and both acquired immunity when they were transformed with the construct. C. divergens LV13 containing the divergicin A signal peptide-carnobacteriocin B2 fusion construct produces both divergicin A and carnobacteriocin B2 and demonstrates the first example of multiple-bacteriocin expression via the general secretory pathway. The small amount of genetic material required for independent bacteriocin expression has implications for the development of a food-grade multiple-bacteriocin expression vector for use in lactic acid bacteria |
| doi_str_mv | 10.1128/aem.62.11.4095-4099.1996 |
| format | Article |
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(University of Alberta, Edmonton, Alberta, Canada.) ; Worobo, R.W ; Stiles, M.E</creator><creatorcontrib>McCormick, J.K. (University of Alberta, Edmonton, Alberta, Canada.) ; Worobo, R.W ; Stiles, M.E</creatorcontrib><description>Carnobacteriocin B2 is a well-characterized class II bacteriocin produced by a 61-kb plasmid from Carnobacterium piscicola LV17. Export of this bacteriocin is dependent on specific ABC (ATP-binding cassette) secretion proteins. Divergicin A is a strongly hydrophobic narrow-spectrum bacteriocin produced by a 3.4kb plasmid from Carnobacterium divergens LV13. Predivergicin A contains a signal peptide and utilizes the general secretary pathway for export (R.W. Worobo, M. J. van Belkum, M. Sailer, K.L. Roy, J. C. Vederas, and M. E. Stiles, J. Bacteriol. 177: 3143-3149, 1995). Fusion of the carnobacteriocin B2 structural gene (devoid of its natural leader peptide) behind the signal peptide of divergicin A in the expression vector pMG36e permitted production and export of active carnobacteriocin B2 in the absence of the specific secretion genes. N-terminal sequencing of purified carnobacteriocin B2 established that correct processing of the prebacteriocin occurred beyond the Ala-Ser-Ala cleavage site of the signal peptide. Carnobacteriocin B2 was produced by the wild-type strain of C divergens, LV13, and in C. piscicola LV17C, the nonbacteriocinogenic, plasmidless variant of the original carnobacteriocin B2 producer strain. The corresponding immunity gene was included immediately downstream of the structural gene. Both of the host strains are sensitive to the bacteriocin, and both acquired immunity when they were transformed with the construct. C. divergens LV13 containing the divergicin A signal peptide-carnobacteriocin B2 fusion construct produces both divergicin A and carnobacteriocin B2 and demonstrates the first example of multiple-bacteriocin expression via the general secretory pathway. The small amount of genetic material required for independent bacteriocin expression has implications for the development of a food-grade multiple-bacteriocin expression vector for use in lactic acid bacteria</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>DOI: 10.1128/aem.62.11.4095-4099.1996</identifier><identifier>PMID: 8900000</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Acids ; ADN RECOMBINADO ; ADN RECOMBINE ; Amino Acid Sequence ; ATP-Binding Cassette Transporters - metabolism ; Bacteria ; Bacterial Proteins - biosynthesis ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; BACTERIAS ACIDOLACTICAS ; BACTERIE LACTIQUE ; BACTERIOCINAS ; BACTERIOCINE ; Bacteriocins - biosynthesis ; Bacteriocins - genetics ; Bacteriocins - metabolism ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Carnobacterium piscicola ; COMPOSICION QUIMICA ; COMPOSITION CHIMIQUE ; DNA Primers - genetics ; DNA, Bacterial - genetics ; Fundamental and applied biological sciences. Psychology ; GENE ; Gene Expression ; GENES ; Genes, Bacterial ; Genetic engineering ; Genetic technics ; GENIE GENETIQUE ; Gram-Positive Asporogenous Rods - genetics ; Gram-Positive Asporogenous Rods - physiology ; INGENIERIA GENETICA ; Methods. Procedures. Technologies ; Microbiology ; Modification of gene expression level ; Molecular Sequence Data ; Peptides ; Plasmids - genetics ; PROPIEDADES ANTIMICROBIANAS ; PROPRIETE ANTIMICROBIENNE ; Protein Sorting Signals - genetics ; Protein Sorting Signals - metabolism ; PROTEINAS ; PROTEINE ; PROTEOLISIS ; PROTEOLYSE ; SECRECION ; SECRETION ; SECUENCIA NUCLEOTIDICA ; SEQUENCE NUCLEOTIDIQUE</subject><ispartof>Applied and Environmental Microbiology, 1996-11, Vol.62 (11), p.4095-4099</ispartof><rights>1997 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Nov 1996</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c668t-eccf32f2ffccef33aea964a5e84d0427099b22f84cda165e8bdf51936409cdcc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC168231/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC168231/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,3175,3176,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2509589$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8900000$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McCormick, J.K. (University of Alberta, Edmonton, Alberta, Canada.)</creatorcontrib><creatorcontrib>Worobo, R.W</creatorcontrib><creatorcontrib>Stiles, M.E</creatorcontrib><title>Expression of the antimicrobial peptide carnobacteriocin B2 by a signal peptide-dependent general secretory pathway</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>Carnobacteriocin B2 is a well-characterized class II bacteriocin produced by a 61-kb plasmid from Carnobacterium piscicola LV17. Export of this bacteriocin is dependent on specific ABC (ATP-binding cassette) secretion proteins. Divergicin A is a strongly hydrophobic narrow-spectrum bacteriocin produced by a 3.4kb plasmid from Carnobacterium divergens LV13. Predivergicin A contains a signal peptide and utilizes the general secretary pathway for export (R.W. Worobo, M. J. van Belkum, M. Sailer, K.L. Roy, J. C. Vederas, and M. E. Stiles, J. Bacteriol. 177: 3143-3149, 1995). Fusion of the carnobacteriocin B2 structural gene (devoid of its natural leader peptide) behind the signal peptide of divergicin A in the expression vector pMG36e permitted production and export of active carnobacteriocin B2 in the absence of the specific secretion genes. N-terminal sequencing of purified carnobacteriocin B2 established that correct processing of the prebacteriocin occurred beyond the Ala-Ser-Ala cleavage site of the signal peptide. Carnobacteriocin B2 was produced by the wild-type strain of C divergens, LV13, and in C. piscicola LV17C, the nonbacteriocinogenic, plasmidless variant of the original carnobacteriocin B2 producer strain. The corresponding immunity gene was included immediately downstream of the structural gene. Both of the host strains are sensitive to the bacteriocin, and both acquired immunity when they were transformed with the construct. C. divergens LV13 containing the divergicin A signal peptide-carnobacteriocin B2 fusion construct produces both divergicin A and carnobacteriocin B2 and demonstrates the first example of multiple-bacteriocin expression via the general secretory pathway. The small amount of genetic material required for independent bacteriocin expression has implications for the development of a food-grade multiple-bacteriocin expression vector for use in lactic acid bacteria</description><subject>Acids</subject><subject>ADN RECOMBINADO</subject><subject>ADN RECOMBINE</subject><subject>Amino Acid Sequence</subject><subject>ATP-Binding Cassette Transporters - metabolism</subject><subject>Bacteria</subject><subject>Bacterial Proteins - biosynthesis</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>BACTERIAS ACIDOLACTICAS</subject><subject>BACTERIE LACTIQUE</subject><subject>BACTERIOCINAS</subject><subject>BACTERIOCINE</subject><subject>Bacteriocins - biosynthesis</subject><subject>Bacteriocins - genetics</subject><subject>Bacteriocins - metabolism</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Carnobacterium piscicola</subject><subject>COMPOSICION QUIMICA</subject><subject>COMPOSITION CHIMIQUE</subject><subject>DNA Primers - genetics</subject><subject>DNA, Bacterial - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENE</subject><subject>Gene Expression</subject><subject>GENES</subject><subject>Genes, Bacterial</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>GENIE GENETIQUE</subject><subject>Gram-Positive Asporogenous Rods - genetics</subject><subject>Gram-Positive Asporogenous Rods - physiology</subject><subject>INGENIERIA GENETICA</subject><subject>Methods. Procedures. Technologies</subject><subject>Microbiology</subject><subject>Modification of gene expression level</subject><subject>Molecular Sequence Data</subject><subject>Peptides</subject><subject>Plasmids - genetics</subject><subject>PROPIEDADES ANTIMICROBIANAS</subject><subject>PROPRIETE ANTIMICROBIENNE</subject><subject>Protein Sorting Signals - genetics</subject><subject>Protein Sorting Signals - metabolism</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEOLISIS</subject><subject>PROTEOLYSE</subject><subject>SECRECION</subject><subject>SECRETION</subject><subject>SECUENCIA NUCLEOTIDICA</subject><subject>SEQUENCE NUCLEOTIDIQUE</subject><issn>0099-2240</issn><issn>1098-5336</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhlcIVELhDyAhWQhx2-CPXa994ABVoUiVOEDP1qx3nLjK2ou9oeTf4yhRSnvBh_Fo5pnxjN-qIowuGePqA-C4lLz4y4bqti5GL5nW8km1YFSruhVCPq0WtMRrzhv6vHqR8y2ltKFSnVVnStP9WVT58s-UMGcfA4mOzGskEGY_epti72FDJpxmPyCxkELswc6YfLQ-kM-c9DsCJPtVuOfqAScMA4aZrDBgKpmMNuEc045MMK_vYPeyeuZgk_HV8T6vbr5c_ry4qq-_f_128em6tlKquUZrneCOO2ctOiEAQcsGWlTNQBveld16zp1q7ABMlnA_uJZpIctv2MFacV59PPSdtv2Igy1DlXnMlPwIaWciePMwE_zarOJvw6TigpX698f6FH9tMc9m9NniZgMB4zabTjVaCSX-C7K26zrRNgV8-wi8jdtUvi8bTlstBGu6AqkDVCTIOaE7Tcyo2atvivpG8uKbvfp7o81e_VL65t-NT4VHuUv-3TEP2cLGJQjW5xPG29JO6fsx1361vvMJDeTx0asFen2AHEQDq1T63PzQHWWUcvEXfyLP4w</recordid><startdate>19961101</startdate><enddate>19961101</enddate><creator>McCormick, J.K. (University of Alberta, Edmonton, Alberta, Canada.)</creator><creator>Worobo, R.W</creator><creator>Stiles, M.E</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19961101</creationdate><title>Expression of the antimicrobial peptide carnobacteriocin B2 by a signal peptide-dependent general secretory pathway</title><author>McCormick, J.K. (University of Alberta, Edmonton, Alberta, Canada.) ; Worobo, R.W ; Stiles, M.E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c668t-eccf32f2ffccef33aea964a5e84d0427099b22f84cda165e8bdf51936409cdcc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Acids</topic><topic>ADN RECOMBINADO</topic><topic>ADN RECOMBINE</topic><topic>Amino Acid Sequence</topic><topic>ATP-Binding Cassette Transporters - metabolism</topic><topic>Bacteria</topic><topic>Bacterial Proteins - biosynthesis</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>BACTERIAS ACIDOLACTICAS</topic><topic>BACTERIE LACTIQUE</topic><topic>BACTERIOCINAS</topic><topic>BACTERIOCINE</topic><topic>Bacteriocins - biosynthesis</topic><topic>Bacteriocins - genetics</topic><topic>Bacteriocins - metabolism</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Carnobacterium piscicola</topic><topic>COMPOSICION QUIMICA</topic><topic>COMPOSITION CHIMIQUE</topic><topic>DNA Primers - genetics</topic><topic>DNA, Bacterial - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENE</topic><topic>Gene Expression</topic><topic>GENES</topic><topic>Genes, Bacterial</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>GENIE GENETIQUE</topic><topic>Gram-Positive Asporogenous Rods - genetics</topic><topic>Gram-Positive Asporogenous Rods - physiology</topic><topic>INGENIERIA GENETICA</topic><topic>Methods. Procedures. Technologies</topic><topic>Microbiology</topic><topic>Modification of gene expression level</topic><topic>Molecular Sequence Data</topic><topic>Peptides</topic><topic>Plasmids - genetics</topic><topic>PROPIEDADES ANTIMICROBIANAS</topic><topic>PROPRIETE ANTIMICROBIENNE</topic><topic>Protein Sorting Signals - genetics</topic><topic>Protein Sorting Signals - metabolism</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEOLISIS</topic><topic>PROTEOLYSE</topic><topic>SECRECION</topic><topic>SECRETION</topic><topic>SECUENCIA NUCLEOTIDICA</topic><topic>SEQUENCE NUCLEOTIDIQUE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McCormick, J.K. (University of Alberta, Edmonton, Alberta, Canada.)</creatorcontrib><creatorcontrib>Worobo, R.W</creatorcontrib><creatorcontrib>Stiles, M.E</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>MEDLINE - Academic</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>McCormick, J.K. (University of Alberta, Edmonton, Alberta, Canada.)</au><au>Worobo, R.W</au><au>Stiles, M.E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of the antimicrobial peptide carnobacteriocin B2 by a signal peptide-dependent general secretory pathway</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>1996-11-01</date><risdate>1996</risdate><volume>62</volume><issue>11</issue><spage>4095</spage><epage>4099</epage><pages>4095-4099</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><coden>AEMIDF</coden><abstract>Carnobacteriocin B2 is a well-characterized class II bacteriocin produced by a 61-kb plasmid from Carnobacterium piscicola LV17. Export of this bacteriocin is dependent on specific ABC (ATP-binding cassette) secretion proteins. Divergicin A is a strongly hydrophobic narrow-spectrum bacteriocin produced by a 3.4kb plasmid from Carnobacterium divergens LV13. Predivergicin A contains a signal peptide and utilizes the general secretary pathway for export (R.W. Worobo, M. J. van Belkum, M. Sailer, K.L. Roy, J. C. Vederas, and M. E. Stiles, J. Bacteriol. 177: 3143-3149, 1995). Fusion of the carnobacteriocin B2 structural gene (devoid of its natural leader peptide) behind the signal peptide of divergicin A in the expression vector pMG36e permitted production and export of active carnobacteriocin B2 in the absence of the specific secretion genes. N-terminal sequencing of purified carnobacteriocin B2 established that correct processing of the prebacteriocin occurred beyond the Ala-Ser-Ala cleavage site of the signal peptide. Carnobacteriocin B2 was produced by the wild-type strain of C divergens, LV13, and in C. piscicola LV17C, the nonbacteriocinogenic, plasmidless variant of the original carnobacteriocin B2 producer strain. The corresponding immunity gene was included immediately downstream of the structural gene. Both of the host strains are sensitive to the bacteriocin, and both acquired immunity when they were transformed with the construct. C. divergens LV13 containing the divergicin A signal peptide-carnobacteriocin B2 fusion construct produces both divergicin A and carnobacteriocin B2 and demonstrates the first example of multiple-bacteriocin expression via the general secretory pathway. The small amount of genetic material required for independent bacteriocin expression has implications for the development of a food-grade multiple-bacteriocin expression vector for use in lactic acid bacteria</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>8900000</pmid><doi>10.1128/aem.62.11.4095-4099.1996</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Applied and Environmental Microbiology, 1996-11, Vol.62 (11), p.4095-4099 |
| issn | 0099-2240 1098-5336 |
| language | eng |
| recordid | cdi_highwire_asm_aem_62_11_4095 |
| source | American Society for Microbiology; MEDLINE; PubMed Central; Alma/SFX Local Collection |
| subjects | Acids ADN RECOMBINADO ADN RECOMBINE Amino Acid Sequence ATP-Binding Cassette Transporters - metabolism Bacteria Bacterial Proteins - biosynthesis Bacterial Proteins - genetics Bacterial Proteins - metabolism BACTERIAS ACIDOLACTICAS BACTERIE LACTIQUE BACTERIOCINAS BACTERIOCINE Bacteriocins - biosynthesis Bacteriocins - genetics Bacteriocins - metabolism Base Sequence Biological and medical sciences Biotechnology Carnobacterium piscicola COMPOSICION QUIMICA COMPOSITION CHIMIQUE DNA Primers - genetics DNA, Bacterial - genetics Fundamental and applied biological sciences. Psychology GENE Gene Expression GENES Genes, Bacterial Genetic engineering Genetic technics GENIE GENETIQUE Gram-Positive Asporogenous Rods - genetics Gram-Positive Asporogenous Rods - physiology INGENIERIA GENETICA Methods. Procedures. Technologies Microbiology Modification of gene expression level Molecular Sequence Data Peptides Plasmids - genetics PROPIEDADES ANTIMICROBIANAS PROPRIETE ANTIMICROBIENNE Protein Sorting Signals - genetics Protein Sorting Signals - metabolism PROTEINAS PROTEINE PROTEOLISIS PROTEOLYSE SECRECION SECRETION SECUENCIA NUCLEOTIDICA SEQUENCE NUCLEOTIDIQUE |
| title | Expression of the antimicrobial peptide carnobacteriocin B2 by a signal peptide-dependent general secretory pathway |
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