Massive Reduction in Methicillin Resistance by Transposon Inactivation of the Normal PBP2 in a Methicillin-Resistant Strain of Staphylococcus aureus
Screening of a large transposon library constructed in the background of a highly and homogeneously methicillin-resistant Staphylococcus aureus (MRSA) strain (methicillin MIC 1,600 μg/ml) for Tn 551 mutants with reduced resistance, identified mutant RUSA130 with a methicillin MIC of 12 μg/ml. Clonin...
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Veröffentlicht in: | Microbial drug resistance (Larchmont, N.Y.) N.Y.), 1997, Vol.3 (4), p.49-413 |
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creator | Pinho, M G Ludovice, A M Wu, S De Lencastre, H |
description | Screening of a large transposon library constructed in the background of a highly and homogeneously methicillin-resistant
Staphylococcus aureus
(MRSA) strain (methicillin MIC 1,600 μg/ml) for Tn
551
mutants with reduced resistance, identified mutant RUSA130 with a methicillin MIC of 12 μg/ml. Cloning in
E. coli
followed by sequencing located the Tn
551
insert Ω703 near the C-terminal of the PBP2 gene. Penicillin-binding assays with mutant RUSA130 showed the presence of normal amounts of penicillin-binding protein 2A (PBP2A) but the absence of PBP2. These observations suggest that the
mecA
gene product PBP2A is not the sole catalyst of peptidoglycan synthesis in MRSA growing in the presence of β-lactam antibiotics, since an intact PBP2 is also essential for the optimal expression of methicillin resistance in MRSA. |
doi_str_mv | 10.1089/mdr.1997.3.409 |
format | Article |
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Staphylococcus aureus
(MRSA) strain (methicillin MIC 1,600 μg/ml) for Tn
551
mutants with reduced resistance, identified mutant RUSA130 with a methicillin MIC of 12 μg/ml. Cloning in
E. coli
followed by sequencing located the Tn
551
insert Ω703 near the C-terminal of the PBP2 gene. Penicillin-binding assays with mutant RUSA130 showed the presence of normal amounts of penicillin-binding protein 2A (PBP2A) but the absence of PBP2. These observations suggest that the
mecA
gene product PBP2A is not the sole catalyst of peptidoglycan synthesis in MRSA growing in the presence of β-lactam antibiotics, since an intact PBP2 is also essential for the optimal expression of methicillin resistance in MRSA.</description><identifier>ISSN: 1076-6294</identifier><identifier>EISSN: 1931-8448</identifier><identifier>DOI: 10.1089/mdr.1997.3.409</identifier><identifier>PMID: 9442495</identifier><language>eng</language><publisher>United States</publisher><subject>Bacterial Proteins ; Bacteriophages - genetics ; Carrier Proteins - immunology ; Culture Media ; DNA Transposable Elements - drug effects ; DNA Transposable Elements - genetics ; DNA, Bacterial - genetics ; DNA, Bacterial - immunology ; Hexosyltransferases ; Methicillin Resistance - genetics ; Muramoylpentapeptide Carboxypeptidase - immunology ; Mutation ; Penicillin-Binding Proteins ; Peptidyl Transferases ; Staphylococcus aureus - drug effects ; Staphylococcus aureus - genetics ; Transduction, Genetic - genetics</subject><ispartof>Microbial drug resistance (Larchmont, N.Y.), 1997, Vol.3 (4), p.49-413</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c366t-895700afdd2871960c1d18da680bd1332d1abd73bc57602146b8def3af29d353</citedby><cites>FETCH-LOGICAL-c366t-895700afdd2871960c1d18da680bd1332d1abd73bc57602146b8def3af29d353</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/mdr.1997.3.409$$EPDF$$P50$$Gmaryannliebert$$H</linktopdf><linktohtml>$$Uhttps://www.liebertpub.com/doi/full/10.1089/mdr.1997.3.409$$EHTML$$P50$$Gmaryannliebert$$H</linktohtml><link.rule.ids>314,780,784,3042,4024,21723,27923,27924,27925,55291,55303</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9442495$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pinho, M G</creatorcontrib><creatorcontrib>Ludovice, A M</creatorcontrib><creatorcontrib>Wu, S</creatorcontrib><creatorcontrib>De Lencastre, H</creatorcontrib><title>Massive Reduction in Methicillin Resistance by Transposon Inactivation of the Normal PBP2 in a Methicillin-Resistant Strain of Staphylococcus aureus</title><title>Microbial drug resistance (Larchmont, N.Y.)</title><addtitle>Microb Drug Resist</addtitle><description>Screening of a large transposon library constructed in the background of a highly and homogeneously methicillin-resistant
Staphylococcus aureus
(MRSA) strain (methicillin MIC 1,600 μg/ml) for Tn
551
mutants with reduced resistance, identified mutant RUSA130 with a methicillin MIC of 12 μg/ml. Cloning in
E. coli
followed by sequencing located the Tn
551
insert Ω703 near the C-terminal of the PBP2 gene. Penicillin-binding assays with mutant RUSA130 showed the presence of normal amounts of penicillin-binding protein 2A (PBP2A) but the absence of PBP2. These observations suggest that the
mecA
gene product PBP2A is not the sole catalyst of peptidoglycan synthesis in MRSA growing in the presence of β-lactam antibiotics, since an intact PBP2 is also essential for the optimal expression of methicillin resistance in MRSA.</description><subject>Bacterial Proteins</subject><subject>Bacteriophages - genetics</subject><subject>Carrier Proteins - immunology</subject><subject>Culture Media</subject><subject>DNA Transposable Elements - drug effects</subject><subject>DNA Transposable Elements - genetics</subject><subject>DNA, Bacterial - genetics</subject><subject>DNA, Bacterial - immunology</subject><subject>Hexosyltransferases</subject><subject>Methicillin Resistance - genetics</subject><subject>Muramoylpentapeptide Carboxypeptidase - immunology</subject><subject>Mutation</subject><subject>Penicillin-Binding Proteins</subject><subject>Peptidyl Transferases</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Staphylococcus aureus - genetics</subject><subject>Transduction, Genetic - genetics</subject><issn>1076-6294</issn><issn>1931-8448</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAURS1EVUphyw7JK3YJduw49hIqCpXaUrWzt15sR2OUxIPtVJr_4IPrdAbEris_-Z17Fu8i9IGSmhKpPk821lSprmY1J-oVOqOK0UpyLl-XmXSiEo3ib9DblH4RQloq2Ck6VZw3XLVn6M8NpOQfHb53djHZhxn7Gd-4vPXGj2OZ713yKcNsHO73eBNhTruQCnc1Qwk8wnMoDDhvHb4NcYIR3329a1YP_G-q_poyfsgR_HPoIcNuux-DCcYsCcMS3ZLeoZMBxuTeH99ztLn8trn4UV3__H518eW6MkyIXEnVdoTAYG0jO6oEMdRSaUFI0lvKWGMp9LZjvWk7QRrKRS-tGxgMjbKsZefo00G7i-H34lLWk0_GjSPMLixJd6pltJH0RbDctHDdaqwPoIkhpegGvYt-grjXlOi1Ll3q0mtdmulSVwl8PJqXfnL2H37sp-z5Yb_-wjyP3vUu5pe0T21SpQA</recordid><startdate>1997</startdate><enddate>1997</enddate><creator>Pinho, M G</creator><creator>Ludovice, A M</creator><creator>Wu, S</creator><creator>De Lencastre, H</creator><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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>1997</creationdate><title>Massive Reduction in Methicillin Resistance by Transposon Inactivation of the Normal PBP2 in a Methicillin-Resistant Strain of Staphylococcus aureus</title><author>Pinho, M G ; Ludovice, A M ; Wu, S ; De Lencastre, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c366t-895700afdd2871960c1d18da680bd1332d1abd73bc57602146b8def3af29d353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Bacterial Proteins</topic><topic>Bacteriophages - genetics</topic><topic>Carrier Proteins - immunology</topic><topic>Culture Media</topic><topic>DNA Transposable Elements - drug effects</topic><topic>DNA Transposable Elements - genetics</topic><topic>DNA, Bacterial - genetics</topic><topic>DNA, Bacterial - immunology</topic><topic>Hexosyltransferases</topic><topic>Methicillin Resistance - genetics</topic><topic>Muramoylpentapeptide Carboxypeptidase - immunology</topic><topic>Mutation</topic><topic>Penicillin-Binding Proteins</topic><topic>Peptidyl Transferases</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Staphylococcus aureus - genetics</topic><topic>Transduction, Genetic - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pinho, M G</creatorcontrib><creatorcontrib>Ludovice, A M</creatorcontrib><creatorcontrib>Wu, S</creatorcontrib><creatorcontrib>De Lencastre, H</creatorcontrib><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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</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>Pinho, M G</au><au>Ludovice, A M</au><au>Wu, S</au><au>De Lencastre, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Massive Reduction in Methicillin Resistance by Transposon Inactivation of the Normal PBP2 in a Methicillin-Resistant Strain of Staphylococcus aureus</atitle><jtitle>Microbial drug resistance (Larchmont, N.Y.)</jtitle><addtitle>Microb Drug Resist</addtitle><date>1997</date><risdate>1997</risdate><volume>3</volume><issue>4</issue><spage>49</spage><epage>413</epage><pages>49-413</pages><issn>1076-6294</issn><eissn>1931-8448</eissn><abstract>Screening of a large transposon library constructed in the background of a highly and homogeneously methicillin-resistant
Staphylococcus aureus
(MRSA) strain (methicillin MIC 1,600 μg/ml) for Tn
551
mutants with reduced resistance, identified mutant RUSA130 with a methicillin MIC of 12 μg/ml. Cloning in
E. coli
followed by sequencing located the Tn
551
insert Ω703 near the C-terminal of the PBP2 gene. Penicillin-binding assays with mutant RUSA130 showed the presence of normal amounts of penicillin-binding protein 2A (PBP2A) but the absence of PBP2. These observations suggest that the
mecA
gene product PBP2A is not the sole catalyst of peptidoglycan synthesis in MRSA growing in the presence of β-lactam antibiotics, since an intact PBP2 is also essential for the optimal expression of methicillin resistance in MRSA.</abstract><cop>United States</cop><pmid>9442495</pmid><doi>10.1089/mdr.1997.3.409</doi><tpages>365</tpages></addata></record> |
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source | Mary Ann Liebert Online Subscription; MEDLINE |
subjects | Bacterial Proteins Bacteriophages - genetics Carrier Proteins - immunology Culture Media DNA Transposable Elements - drug effects DNA Transposable Elements - genetics DNA, Bacterial - genetics DNA, Bacterial - immunology Hexosyltransferases Methicillin Resistance - genetics Muramoylpentapeptide Carboxypeptidase - immunology Mutation Penicillin-Binding Proteins Peptidyl Transferases Staphylococcus aureus - drug effects Staphylococcus aureus - genetics Transduction, Genetic - genetics |
title | Massive Reduction in Methicillin Resistance by Transposon Inactivation of the Normal PBP2 in a Methicillin-Resistant Strain of Staphylococcus aureus |
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