Spontaneous Nisin-Resistant Listeria monocytogenes Mutants with Increased Expression of a Putative Penicillin-Binding Protein and Their Sensitivity to Various Antibiotics
A concern regarding the use of bacteriocins, as for example the lantibiotic nisin, for biopreservation of certain food products is the possibility of resistance development and potential cross-resistance to antibiotics in the target organism. The genetic basis for nisin resistance development is as...
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| Veröffentlicht in: | Microbial drug resistance (Larchmont, N.Y.) N.Y.), 2001-06, Vol.7 (2), p.127-135 |
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| description | A concern regarding the use of bacteriocins, as for example the lantibiotic nisin, for biopreservation of certain food products is the possibility of resistance development and potential cross-resistance
to antibiotics in the target organism. The genetic basis for nisin resistance development is as yet unknown. We analyzed changes in gene expression following nisin resistance development in
Listeria
monocytogenes
412 by restriction fragment differential display. The mutant had increased expression of a protein with strong homology to the glycosyltransferase domain of high-molecular-weight penicillin-binding
proteins (PBPs), a histidine protein kinase, a protein of unknown function, and ClpB (putative functions from homology). The three former proteins had increased expression in a total of six out of 10 independent
mutants originating from five different wild-type strains, indicating a prevalent nisin resistance mechanism under the employed isolation conditions. Increased expression of the putative PBP may affect
the cell wall composition and thereby alter the sensitivity to cell wall-targeting compounds. The mutants had an isolate-specific increase in sensitivity to different β-lactams and a slight decrease
in sensitivity to another lantibiotic, mersacidin. A model incorporating these observations is proposed based on current knowledge of nisin's mode of action. |
| doi_str_mv | 10.1089/10766290152045002 |
| format | Article |
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to antibiotics in the target organism. The genetic basis for nisin resistance development is as yet unknown. We analyzed changes in gene expression following nisin resistance development in
Listeria
monocytogenes
412 by restriction fragment differential display. The mutant had increased expression of a protein with strong homology to the glycosyltransferase domain of high-molecular-weight penicillin-binding
proteins (PBPs), a histidine protein kinase, a protein of unknown function, and ClpB (putative functions from homology). The three former proteins had increased expression in a total of six out of 10 independent
mutants originating from five different wild-type strains, indicating a prevalent nisin resistance mechanism under the employed isolation conditions. Increased expression of the putative PBP may affect
the cell wall composition and thereby alter the sensitivity to cell wall-targeting compounds. The mutants had an isolate-specific increase in sensitivity to different β-lactams and a slight decrease
in sensitivity to another lantibiotic, mersacidin. A model incorporating these observations is proposed based on current knowledge of nisin's mode of action.</description><identifier>ISSN: 1076-6294</identifier><identifier>EISSN: 1931-8448</identifier><identifier>DOI: 10.1089/10766290152045002</identifier><identifier>PMID: 11442339</identifier><language>eng</language><publisher>United States: Mary Ann Liebert, Inc</publisher><subject>Anti-Bacterial Agents - pharmacology ; Antibiotics ; Bacterial Proteins ; Blotting, Northern ; Carrier Proteins - biosynthesis ; Carrier Proteins - genetics ; DNA, Bacterial - chemistry ; DNA, Bacterial - genetics ; Drug Resistance, Microbial ; Hexosyltransferases ; Lipids - chemistry ; Listeria monocytogenes ; Listeria monocytogenes - chemistry ; Listeria monocytogenes - drug effects ; Listeria monocytogenes - genetics ; Mechanisms ; mersacidin ; Microbial Sensitivity Tests ; Mode of action ; Muramoylpentapeptide Carboxypeptidase - biosynthesis ; Muramoylpentapeptide Carboxypeptidase - genetics ; Mutants ; Mutation ; Nisin - pharmacology ; Penicillin-Binding Proteins ; Peptidyl Transferases ; Polymorphism, Restriction Fragment Length ; Proteins ; Reverse Transcriptase Polymerase Chain Reaction</subject><ispartof>Microbial drug resistance (Larchmont, N.Y.), 2001-06, Vol.7 (2), p.127-135</ispartof><rights>Copyright Mary Ann Liebert Inc. Jun 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c403t-9615bcbe9589193bcba4df269d1d4fe0c849b939120191df78f2f819a7e871f63</citedby><cites>FETCH-LOGICAL-c403t-9615bcbe9589193bcba4df269d1d4fe0c849b939120191df78f2f819a7e871f63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.liebertpub.com/doi/epdf/10.1089/10766290152045002$$EPDF$$P50$$Gmaryannliebert$$H</linktopdf><linktohtml>$$Uhttps://www.liebertpub.com/doi/full/10.1089/10766290152045002$$EHTML$$P50$$Gmaryannliebert$$H</linktohtml><link.rule.ids>314,780,784,3042,21723,27924,27925,55291,55303</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11442339$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gravesen, Anne</creatorcontrib><creatorcontrib>Sørensen, Karen</creatorcontrib><creatorcontrib>Aarestrup, Frank M.</creatorcontrib><creatorcontrib>Knøchel, Susanne</creatorcontrib><title>Spontaneous Nisin-Resistant Listeria monocytogenes Mutants with Increased Expression of a Putative Penicillin-Binding Protein and Their Sensitivity to Various Antibiotics</title><title>Microbial drug resistance (Larchmont, N.Y.)</title><addtitle>Microb Drug Resist</addtitle><description>A concern regarding the use of bacteriocins, as for example the lantibiotic nisin, for biopreservation of certain food products is the possibility of resistance development and potential cross-resistance
to antibiotics in the target organism. The genetic basis for nisin resistance development is as yet unknown. We analyzed changes in gene expression following nisin resistance development in
Listeria
monocytogenes
412 by restriction fragment differential display. The mutant had increased expression of a protein with strong homology to the glycosyltransferase domain of high-molecular-weight penicillin-binding
proteins (PBPs), a histidine protein kinase, a protein of unknown function, and ClpB (putative functions from homology). The three former proteins had increased expression in a total of six out of 10 independent
mutants originating from five different wild-type strains, indicating a prevalent nisin resistance mechanism under the employed isolation conditions. Increased expression of the putative PBP may affect
the cell wall composition and thereby alter the sensitivity to cell wall-targeting compounds. The mutants had an isolate-specific increase in sensitivity to different β-lactams and a slight decrease
in sensitivity to another lantibiotic, mersacidin. A model incorporating these observations is proposed based on current knowledge of nisin's mode of action.</description><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibiotics</subject><subject>Bacterial Proteins</subject><subject>Blotting, Northern</subject><subject>Carrier Proteins - biosynthesis</subject><subject>Carrier Proteins - genetics</subject><subject>DNA, Bacterial - chemistry</subject><subject>DNA, Bacterial - genetics</subject><subject>Drug Resistance, Microbial</subject><subject>Hexosyltransferases</subject><subject>Lipids - chemistry</subject><subject>Listeria monocytogenes</subject><subject>Listeria monocytogenes - chemistry</subject><subject>Listeria monocytogenes - drug effects</subject><subject>Listeria monocytogenes - genetics</subject><subject>Mechanisms</subject><subject>mersacidin</subject><subject>Microbial Sensitivity Tests</subject><subject>Mode of action</subject><subject>Muramoylpentapeptide Carboxypeptidase - biosynthesis</subject><subject>Muramoylpentapeptide Carboxypeptidase - genetics</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Nisin - pharmacology</subject><subject>Penicillin-Binding Proteins</subject><subject>Peptidyl Transferases</subject><subject>Polymorphism, Restriction Fragment Length</subject><subject>Proteins</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><issn>1076-6294</issn><issn>1931-8448</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkc9uFDEMxiMEoqXwAFxQxIHbQDyT-ZNjqQpUWmBFC9dRJuO0rmaTJcnQ7ivxlGS0KyHBAU627J8_2f4Yew7iNYhOvQHRNk2pBNSlkLUQ5QN2DKqCopOye5jz3C8yII_YkxhvhRA1NNVjdgQgZVlV6pj9vNx6l7RDP0f-iSK54gtGirmU-CpHDKT5xjtvdslfo8PIP85LN_I7Sjf8wpmAOuLIz--3AWMk77i3XPN1xhL9QL5GR4amKWu_JTeSu-br4BOS49qN_OoGKfBLdJEyTmnHk-ffdKBlpVOXaCCfyMSn7JHVU8Rnh3jCvr47vzr7UKw-v784O10VRooqFaqBejADqrpT-Rk51XK0ZaNGGKVFYTqpBlUpKAUoGG3b2dJ2oHSLXQu2qU7Yq73uNvjvM8bUbyganKb9l_pWqFYJJf8JQidaJZs2gy__AG_9HFw-os_GqbKpmkUN9pAJPsaAtt8G2uiw60H0i939X3bnmRcH4XnY4Ph74uBvBto9sJS1cxPhgCH9h_Qv-R25cg</recordid><startdate>20010601</startdate><enddate>20010601</enddate><creator>Gravesen, Anne</creator><creator>Sørensen, Karen</creator><creator>Aarestrup, Frank M.</creator><creator>Knøchel, Susanne</creator><general>Mary Ann Liebert, Inc</general><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>7QP</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</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>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20010601</creationdate><title>Spontaneous Nisin-Resistant Listeria monocytogenes Mutants with Increased Expression of a Putative Penicillin-Binding Protein and Their Sensitivity to Various Antibiotics</title><author>Gravesen, Anne ; Sørensen, Karen ; Aarestrup, Frank M. ; Knøchel, Susanne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c403t-9615bcbe9589193bcba4df269d1d4fe0c849b939120191df78f2f819a7e871f63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antibiotics</topic><topic>Bacterial Proteins</topic><topic>Blotting, Northern</topic><topic>Carrier Proteins - biosynthesis</topic><topic>Carrier Proteins - genetics</topic><topic>DNA, Bacterial - chemistry</topic><topic>DNA, Bacterial - genetics</topic><topic>Drug Resistance, Microbial</topic><topic>Hexosyltransferases</topic><topic>Lipids - chemistry</topic><topic>Listeria monocytogenes</topic><topic>Listeria monocytogenes - chemistry</topic><topic>Listeria monocytogenes - drug effects</topic><topic>Listeria monocytogenes - genetics</topic><topic>Mechanisms</topic><topic>mersacidin</topic><topic>Microbial Sensitivity Tests</topic><topic>Mode of action</topic><topic>Muramoylpentapeptide Carboxypeptidase - biosynthesis</topic><topic>Muramoylpentapeptide Carboxypeptidase - genetics</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Nisin - pharmacology</topic><topic>Penicillin-Binding Proteins</topic><topic>Peptidyl Transferases</topic><topic>Polymorphism, Restriction Fragment Length</topic><topic>Proteins</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gravesen, Anne</creatorcontrib><creatorcontrib>Sørensen, Karen</creatorcontrib><creatorcontrib>Aarestrup, Frank M.</creatorcontrib><creatorcontrib>Knøchel, Susanne</creatorcontrib><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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</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 Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>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>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>Science 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>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Microbial drug resistance (Larchmont, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gravesen, Anne</au><au>Sørensen, Karen</au><au>Aarestrup, Frank M.</au><au>Knøchel, Susanne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Spontaneous Nisin-Resistant Listeria monocytogenes Mutants with Increased Expression of a Putative Penicillin-Binding Protein and Their Sensitivity to Various Antibiotics</atitle><jtitle>Microbial drug resistance (Larchmont, N.Y.)</jtitle><addtitle>Microb Drug Resist</addtitle><date>2001-06-01</date><risdate>2001</risdate><volume>7</volume><issue>2</issue><spage>127</spage><epage>135</epage><pages>127-135</pages><issn>1076-6294</issn><eissn>1931-8448</eissn><abstract>A concern regarding the use of bacteriocins, as for example the lantibiotic nisin, for biopreservation of certain food products is the possibility of resistance development and potential cross-resistance
to antibiotics in the target organism. The genetic basis for nisin resistance development is as yet unknown. We analyzed changes in gene expression following nisin resistance development in
Listeria
monocytogenes
412 by restriction fragment differential display. The mutant had increased expression of a protein with strong homology to the glycosyltransferase domain of high-molecular-weight penicillin-binding
proteins (PBPs), a histidine protein kinase, a protein of unknown function, and ClpB (putative functions from homology). The three former proteins had increased expression in a total of six out of 10 independent
mutants originating from five different wild-type strains, indicating a prevalent nisin resistance mechanism under the employed isolation conditions. Increased expression of the putative PBP may affect
the cell wall composition and thereby alter the sensitivity to cell wall-targeting compounds. The mutants had an isolate-specific increase in sensitivity to different β-lactams and a slight decrease
in sensitivity to another lantibiotic, mersacidin. A model incorporating these observations is proposed based on current knowledge of nisin's mode of action.</abstract><cop>United States</cop><pub>Mary Ann Liebert, Inc</pub><pmid>11442339</pmid><doi>10.1089/10766290152045002</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1076-6294 |
| ispartof | Microbial drug resistance (Larchmont, N.Y.), 2001-06, Vol.7 (2), p.127-135 |
| issn | 1076-6294 1931-8448 |
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| source | Mary Ann Liebert Online Subscription; MEDLINE |
| subjects | Anti-Bacterial Agents - pharmacology Antibiotics Bacterial Proteins Blotting, Northern Carrier Proteins - biosynthesis Carrier Proteins - genetics DNA, Bacterial - chemistry DNA, Bacterial - genetics Drug Resistance, Microbial Hexosyltransferases Lipids - chemistry Listeria monocytogenes Listeria monocytogenes - chemistry Listeria monocytogenes - drug effects Listeria monocytogenes - genetics Mechanisms mersacidin Microbial Sensitivity Tests Mode of action Muramoylpentapeptide Carboxypeptidase - biosynthesis Muramoylpentapeptide Carboxypeptidase - genetics Mutants Mutation Nisin - pharmacology Penicillin-Binding Proteins Peptidyl Transferases Polymorphism, Restriction Fragment Length Proteins Reverse Transcriptase Polymerase Chain Reaction |
| title | Spontaneous Nisin-Resistant Listeria monocytogenes Mutants with Increased Expression of a Putative Penicillin-Binding Protein and Their Sensitivity to Various Antibiotics |
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