Differential Inhibition of Staphylococcus aureus PBP2 by Glycopeptide Antibiotics
The glycopeptide antibiotics prevent maturation of the bacterial cell wall by binding to the terminal d-alanyl-d-alanine moiety of peptidoglycan precursors, thereby inhibiting the enzymes involved in the final stages of peptidoglycan synthesis. However, there are significant differences in the biolo...
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| Veröffentlicht in: | Journal of the American Chemical Society 2005-03, Vol.127 (10), p.3250-3251 |
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| container_title | Journal of the American Chemical Society |
| container_volume | 127 |
| creator | Leimkuhler, Catherine Chen, Lan Barrett, Dianah Panzone, Gianbattista Sun, Binyuan Falcone, Brian Oberthür, Markus Donadio, Stefano Walker, Suzanne Kahne, Daniel |
| description | The glycopeptide antibiotics prevent maturation of the bacterial cell wall by binding to the terminal d-alanyl-d-alanine moiety of peptidoglycan precursors, thereby inhibiting the enzymes involved in the final stages of peptidoglycan synthesis. However, there are significant differences in the biological activity of particular glycopeptide derivatives that are not related to their affinity for d-Ala-d-Ala. We compare the ability of vancomycin and a set of clinically relevant glycopeptides to inhibit Staphylococcus aureus PBP2 (penicillin binding protein), the major transglycosylase in a clinically relevant pathogen, S. aureus. We report experiments suggesting that activity differences between glycopeptides against this organism reflect a combination of substrate binding and secondary interactions with key enzymes involved in peptidoglycan synthesis. |
| doi_str_mv | 10.1021/ja043849e |
| format | Article |
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However, there are significant differences in the biological activity of particular glycopeptide derivatives that are not related to their affinity for d-Ala-d-Ala. We compare the ability of vancomycin and a set of clinically relevant glycopeptides to inhibit Staphylococcus aureus PBP2 (penicillin binding protein), the major transglycosylase in a clinically relevant pathogen, S. aureus. We report experiments suggesting that activity differences between glycopeptides against this organism reflect a combination of substrate binding and secondary interactions with key enzymes involved in peptidoglycan synthesis.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja043849e</identifier><identifier>PMID: 15755121</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Action of physical and chemical agents on bacteria ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - metabolism ; Anti-Bacterial Agents - pharmacology ; Bacteriology ; Biological and medical sciences ; Dipeptides - chemistry ; Dipeptides - metabolism ; Fundamental and applied biological sciences. Psychology ; General pharmacology ; Kinetics ; Medical sciences ; Microbial Sensitivity Tests ; Microbiology ; Penicillin-Binding Proteins - antagonists & inhibitors ; Penicillin-Binding Proteins - chemistry ; Penicillin-Binding Proteins - metabolism ; Pharmacology. Drug treatments ; Physicochemical properties. Structure-activity relationships ; Staphylococcus aureus - drug effects ; Staphylococcus aureus - enzymology ; Substrate Specificity ; Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives ; Uridine Diphosphate N-Acetylmuramic Acid - chemistry ; Uridine Diphosphate N-Acetylmuramic Acid - metabolism ; Vancomycin - chemistry ; Vancomycin - metabolism ; Vancomycin - pharmacology</subject><ispartof>Journal of the American Chemical Society, 2005-03, Vol.127 (10), p.3250-3251</ispartof><rights>Copyright © 2005 American Chemical Society</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a478t-d17974c59cdf05d0c751c1efd3703a36391e68514916598dd013da685de53e0d3</citedby><cites>FETCH-LOGICAL-a478t-d17974c59cdf05d0c751c1efd3703a36391e68514916598dd013da685de53e0d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ja043849e$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ja043849e$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16758600$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15755121$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leimkuhler, Catherine</creatorcontrib><creatorcontrib>Chen, Lan</creatorcontrib><creatorcontrib>Barrett, Dianah</creatorcontrib><creatorcontrib>Panzone, Gianbattista</creatorcontrib><creatorcontrib>Sun, Binyuan</creatorcontrib><creatorcontrib>Falcone, Brian</creatorcontrib><creatorcontrib>Oberthür, Markus</creatorcontrib><creatorcontrib>Donadio, Stefano</creatorcontrib><creatorcontrib>Walker, Suzanne</creatorcontrib><creatorcontrib>Kahne, Daniel</creatorcontrib><title>Differential Inhibition of Staphylococcus aureus PBP2 by Glycopeptide Antibiotics</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>The glycopeptide antibiotics prevent maturation of the bacterial cell wall by binding to the terminal d-alanyl-d-alanine moiety of peptidoglycan precursors, thereby inhibiting the enzymes involved in the final stages of peptidoglycan synthesis. However, there are significant differences in the biological activity of particular glycopeptide derivatives that are not related to their affinity for d-Ala-d-Ala. We compare the ability of vancomycin and a set of clinically relevant glycopeptides to inhibit Staphylococcus aureus PBP2 (penicillin binding protein), the major transglycosylase in a clinically relevant pathogen, S. aureus. We report experiments suggesting that activity differences between glycopeptides against this organism reflect a combination of substrate binding and secondary interactions with key enzymes involved in peptidoglycan synthesis.</description><subject>Action of physical and chemical agents on bacteria</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - metabolism</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Dipeptides - chemistry</subject><subject>Dipeptides - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General pharmacology</subject><subject>Kinetics</subject><subject>Medical sciences</subject><subject>Microbial Sensitivity Tests</subject><subject>Microbiology</subject><subject>Penicillin-Binding Proteins - antagonists & inhibitors</subject><subject>Penicillin-Binding Proteins - chemistry</subject><subject>Penicillin-Binding Proteins - metabolism</subject><subject>Pharmacology. Drug treatments</subject><subject>Physicochemical properties. Structure-activity relationships</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Staphylococcus aureus - enzymology</subject><subject>Substrate Specificity</subject><subject>Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives</subject><subject>Uridine Diphosphate N-Acetylmuramic Acid - chemistry</subject><subject>Uridine Diphosphate N-Acetylmuramic Acid - metabolism</subject><subject>Vancomycin - chemistry</subject><subject>Vancomycin - metabolism</subject><subject>Vancomycin - pharmacology</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0D1v2zAQBmCiaNA4Tof-gUJLA2RQwhNFURrz_YEgsWG3HQmaPCF0ZVEhJSD-92FgI14KZDqQfHi4ewn5AfQEaAanS0VzVuYVfiEj4BlNOWTFVzKilGapKAu2Tw5CWMZjnpXwjewDFzwaGJHppa1r9Nj2VjXJXftsF7a3rk1cncx61T2vG6ed1kNI1OAxlsn5JEsW6-SmWWvXYddbg8lZ_L-wrrc6HJK9WjUBv2_rmPy-vppf3KYPTzd3F2cPqcpF2acGRCVyzSttasoN1YKDBqwNE5QpVrAKsCg55BUUvCqNocCMijcGOUNq2Jgcbfp23r0MGHq5skFj06gW3RBkIThloso_hSAKnjOeRXi8gdq7EDzWsvN2pfxaApXvQcuPoKP9uW06LFZodnKbbAS_tkAFrZraq1bbsHNxvLKgNLp042zo8fXjXfl_cQMmuJxPZnLC_04f4fpe_tn1VTrIpRt8G0P-z4Bv-ROfjw</recordid><startdate>20050316</startdate><enddate>20050316</enddate><creator>Leimkuhler, Catherine</creator><creator>Chen, Lan</creator><creator>Barrett, Dianah</creator><creator>Panzone, Gianbattista</creator><creator>Sun, Binyuan</creator><creator>Falcone, Brian</creator><creator>Oberthür, Markus</creator><creator>Donadio, Stefano</creator><creator>Walker, Suzanne</creator><creator>Kahne, Daniel</creator><general>American Chemical Society</general><scope>BSCLL</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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20050316</creationdate><title>Differential Inhibition of Staphylococcus aureus PBP2 by Glycopeptide Antibiotics</title><author>Leimkuhler, Catherine ; Chen, Lan ; Barrett, Dianah ; Panzone, Gianbattista ; Sun, Binyuan ; Falcone, Brian ; Oberthür, Markus ; Donadio, Stefano ; Walker, Suzanne ; Kahne, Daniel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a478t-d17974c59cdf05d0c751c1efd3703a36391e68514916598dd013da685de53e0d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Action of physical and chemical agents on bacteria</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>Anti-Bacterial Agents - metabolism</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Dipeptides - chemistry</topic><topic>Dipeptides - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General pharmacology</topic><topic>Kinetics</topic><topic>Medical sciences</topic><topic>Microbial Sensitivity Tests</topic><topic>Microbiology</topic><topic>Penicillin-Binding Proteins - antagonists & inhibitors</topic><topic>Penicillin-Binding Proteins - chemistry</topic><topic>Penicillin-Binding Proteins - metabolism</topic><topic>Pharmacology. Drug treatments</topic><topic>Physicochemical properties. Structure-activity relationships</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Staphylococcus aureus - enzymology</topic><topic>Substrate Specificity</topic><topic>Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives</topic><topic>Uridine Diphosphate N-Acetylmuramic Acid - chemistry</topic><topic>Uridine Diphosphate N-Acetylmuramic Acid - metabolism</topic><topic>Vancomycin - chemistry</topic><topic>Vancomycin - metabolism</topic><topic>Vancomycin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leimkuhler, Catherine</creatorcontrib><creatorcontrib>Chen, Lan</creatorcontrib><creatorcontrib>Barrett, Dianah</creatorcontrib><creatorcontrib>Panzone, Gianbattista</creatorcontrib><creatorcontrib>Sun, Binyuan</creatorcontrib><creatorcontrib>Falcone, Brian</creatorcontrib><creatorcontrib>Oberthür, Markus</creatorcontrib><creatorcontrib>Donadio, Stefano</creatorcontrib><creatorcontrib>Walker, Suzanne</creatorcontrib><creatorcontrib>Kahne, Daniel</creatorcontrib><collection>Istex</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>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>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leimkuhler, Catherine</au><au>Chen, Lan</au><au>Barrett, Dianah</au><au>Panzone, Gianbattista</au><au>Sun, Binyuan</au><au>Falcone, Brian</au><au>Oberthür, Markus</au><au>Donadio, Stefano</au><au>Walker, Suzanne</au><au>Kahne, Daniel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential Inhibition of Staphylococcus aureus PBP2 by Glycopeptide Antibiotics</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2005-03-16</date><risdate>2005</risdate><volume>127</volume><issue>10</issue><spage>3250</spage><epage>3251</epage><pages>3250-3251</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>The glycopeptide antibiotics prevent maturation of the bacterial cell wall by binding to the terminal d-alanyl-d-alanine moiety of peptidoglycan precursors, thereby inhibiting the enzymes involved in the final stages of peptidoglycan synthesis. However, there are significant differences in the biological activity of particular glycopeptide derivatives that are not related to their affinity for d-Ala-d-Ala. We compare the ability of vancomycin and a set of clinically relevant glycopeptides to inhibit Staphylococcus aureus PBP2 (penicillin binding protein), the major transglycosylase in a clinically relevant pathogen, S. aureus. We report experiments suggesting that activity differences between glycopeptides against this organism reflect a combination of substrate binding and secondary interactions with key enzymes involved in peptidoglycan synthesis.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>15755121</pmid><doi>10.1021/ja043849e</doi><tpages>2</tpages></addata></record> |
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| subjects | Action of physical and chemical agents on bacteria Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology Bacteriology Biological and medical sciences Dipeptides - chemistry Dipeptides - metabolism Fundamental and applied biological sciences. Psychology General pharmacology Kinetics Medical sciences Microbial Sensitivity Tests Microbiology Penicillin-Binding Proteins - antagonists & inhibitors Penicillin-Binding Proteins - chemistry Penicillin-Binding Proteins - metabolism Pharmacology. Drug treatments Physicochemical properties. Structure-activity relationships Staphylococcus aureus - drug effects Staphylococcus aureus - enzymology Substrate Specificity Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives Uridine Diphosphate N-Acetylmuramic Acid - chemistry Uridine Diphosphate N-Acetylmuramic Acid - metabolism Vancomycin - chemistry Vancomycin - metabolism Vancomycin - pharmacology |
| title | Differential Inhibition of Staphylococcus aureus PBP2 by Glycopeptide Antibiotics |
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