The anti-MRSA compound 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) inhibits protein synthesis in Staphylococcus aureus
Methicillin-resistant S aureus (MRSA) contributes to patient mortality and extended hospital stays. 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) is a natural product antibiotic that is effective against MRSA but has no known mechanism of action (MOA). We used proteomics to identify the MOA for...
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| Veröffentlicht in: | Journal of proteomics 2020-01, Vol.210, p.103539-103539, Article 103539 |
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| creator | Carruthers, Nicholas J. Stemmer, Paul M. Media, Joe Swartz, Ken Wang, Xiaojuan Aube, Nicholas Hamann, Mark T. Valeriote, Frederick Shaw, Jiajiu |
| description | Methicillin-resistant S aureus (MRSA) contributes to patient mortality and extended hospital stays. 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) is a natural product antibiotic that is effective against MRSA but has no known mechanism of action (MOA). We used proteomics to identify the MOA for KCR.
Methicillin sensitive S aureus and a mixture of four KCR stereoisomers were tested. A time-kill assay was used to choose a 4 h treatment using KCR at 5× its MIC for proteomic analysis. S aureus was treated in triplicate with KCR, oxacillin or vehicle and quantitative proteomic analysis was carried out using isobaric tags and mass spectrometry. 1190 proteins were identified and 552 were affected by KCR (q |
| doi_str_mv | 10.1016/j.jprot.2019.103539 |
| format | Article |
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Methicillin sensitive S aureus and a mixture of four KCR stereoisomers were tested. A time-kill assay was used to choose a 4 h treatment using KCR at 5× its MIC for proteomic analysis. S aureus was treated in triplicate with KCR, oxacillin or vehicle and quantitative proteomic analysis was carried out using isobaric tags and mass spectrometry. 1190 proteins were identified and 552 were affected by KCR (q < 0.01). Ontology analysis identified 6 distinct translation-related categories that were affected by KCR (PIANO, 10% false-discovery rate) including structural constituent of ribosome, translation, rRNA binding, tRNA binding, tRNA processing and aminoacyl-tRNA ligase activity. Median fold changes (KCR vs Control) for small and large ribosomal components were 1.46 and 1.43 respectively. KCR inhibited the production of luciferase protein in an in vitro assay (IC50 39.6 μg/ml).
Upregulation of translation-related proteins in response to KCR indicates that KCR acts to disrupt S aureus protein synthesis. This was confirmed with an in vitro transcription/translation assay.
Methicillin-resistant S aureus (MRSA) contributes to patient mortality and extended hospital stays. 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) is a natural product antibiotic that is effective against MRSA but has no known mechanism of action (MOA). Using proteomic analysis we determined that KCR acts by inhibiting protein synthesis. KCR is an exciting novel antibiotic and this work represents an important step in its development towards clinical use.
[Display omitted]
•A mixture of KCR isomers ZZ, EZ, ZE and EE was tested for antimicrobial activity against methicillin-sensitive S aureus.•Translation-associated proteins were increased after KCR treatment suggesting that KCR acts to inhibit translation.•An in vitro translation assay supported the proposed mechanism.</description><identifier>ISSN: 1874-3919</identifier><identifier>EISSN: 1876-7737</identifier><identifier>DOI: 10.1016/j.jprot.2019.103539</identifier><identifier>PMID: 31629958</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside ; aminoacyl tRNA ligases ; Anti-Bacterial Agents - pharmacology ; antibiotic resistance ; Bacterial Proteins - metabolism ; enzyme activity ; hospitals ; Humans ; in vitro studies ; inhibitory concentration 50 ; Kaempferols - pharmacology ; KCR ; luciferase ; mass spectrometry ; Mechanism of action ; methicillin ; Methicillin-resistant ; methicillin-resistant Staphylococcus aureus ; Methicillin-Resistant Staphylococcus aureus - drug effects ; Methicillin-Resistant Staphylococcus aureus - isolation & purification ; Methicillin-Resistant Staphylococcus aureus - metabolism ; Microbial Sensitivity Tests - methods ; mortality ; oxacillin ; patients ; Protein Biosynthesis ; protein synthesis ; Protein Synthesis Inhibitors - pharmacology ; Proteomics ; Proteomics - methods ; Rhamnose - analogs & derivatives ; Rhamnose - pharmacology ; ribosomal RNA ; ribosomes ; Staphylococcal Infections - drug therapy ; Staphylococcal Infections - metabolism ; Staphylococcal Infections - microbiology ; Staphylococcus aureus ; stereoisomers ; translation (genetics)</subject><ispartof>Journal of proteomics, 2020-01, Vol.210, p.103539-103539, Article 103539</ispartof><rights>2019 Elsevier B.V.</rights><rights>Copyright © 2019 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-ce5be6bb520cdc606a03540bcdf85aab352d31a2c980e1ed335a7bc6569ece223</citedby><cites>FETCH-LOGICAL-c492t-ce5be6bb520cdc606a03540bcdf85aab352d31a2c980e1ed335a7bc6569ece223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1874391919303112$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31629958$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Carruthers, Nicholas J.</creatorcontrib><creatorcontrib>Stemmer, Paul M.</creatorcontrib><creatorcontrib>Media, Joe</creatorcontrib><creatorcontrib>Swartz, Ken</creatorcontrib><creatorcontrib>Wang, Xiaojuan</creatorcontrib><creatorcontrib>Aube, Nicholas</creatorcontrib><creatorcontrib>Hamann, Mark T.</creatorcontrib><creatorcontrib>Valeriote, Frederick</creatorcontrib><creatorcontrib>Shaw, Jiajiu</creatorcontrib><title>The anti-MRSA compound 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) inhibits protein synthesis in Staphylococcus aureus</title><title>Journal of proteomics</title><addtitle>J Proteomics</addtitle><description>Methicillin-resistant S aureus (MRSA) contributes to patient mortality and extended hospital stays. 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) is a natural product antibiotic that is effective against MRSA but has no known mechanism of action (MOA). We used proteomics to identify the MOA for KCR.
Methicillin sensitive S aureus and a mixture of four KCR stereoisomers were tested. A time-kill assay was used to choose a 4 h treatment using KCR at 5× its MIC for proteomic analysis. S aureus was treated in triplicate with KCR, oxacillin or vehicle and quantitative proteomic analysis was carried out using isobaric tags and mass spectrometry. 1190 proteins were identified and 552 were affected by KCR (q < 0.01). Ontology analysis identified 6 distinct translation-related categories that were affected by KCR (PIANO, 10% false-discovery rate) including structural constituent of ribosome, translation, rRNA binding, tRNA binding, tRNA processing and aminoacyl-tRNA ligase activity. Median fold changes (KCR vs Control) for small and large ribosomal components were 1.46 and 1.43 respectively. KCR inhibited the production of luciferase protein in an in vitro assay (IC50 39.6 μg/ml).
Upregulation of translation-related proteins in response to KCR indicates that KCR acts to disrupt S aureus protein synthesis. This was confirmed with an in vitro transcription/translation assay.
Methicillin-resistant S aureus (MRSA) contributes to patient mortality and extended hospital stays. 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) is a natural product antibiotic that is effective against MRSA but has no known mechanism of action (MOA). Using proteomic analysis we determined that KCR acts by inhibiting protein synthesis. KCR is an exciting novel antibiotic and this work represents an important step in its development towards clinical use.
[Display omitted]
•A mixture of KCR isomers ZZ, EZ, ZE and EE was tested for antimicrobial activity against methicillin-sensitive S aureus.•Translation-associated proteins were increased after KCR treatment suggesting that KCR acts to inhibit translation.•An in vitro translation assay supported the proposed mechanism.</description><subject>3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside</subject><subject>aminoacyl tRNA ligases</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>antibiotic resistance</subject><subject>Bacterial Proteins - metabolism</subject><subject>enzyme activity</subject><subject>hospitals</subject><subject>Humans</subject><subject>in vitro studies</subject><subject>inhibitory concentration 50</subject><subject>Kaempferols - pharmacology</subject><subject>KCR</subject><subject>luciferase</subject><subject>mass spectrometry</subject><subject>Mechanism of action</subject><subject>methicillin</subject><subject>Methicillin-resistant</subject><subject>methicillin-resistant Staphylococcus aureus</subject><subject>Methicillin-Resistant Staphylococcus aureus - drug effects</subject><subject>Methicillin-Resistant Staphylococcus aureus - isolation & purification</subject><subject>Methicillin-Resistant Staphylococcus aureus - metabolism</subject><subject>Microbial Sensitivity Tests - methods</subject><subject>mortality</subject><subject>oxacillin</subject><subject>patients</subject><subject>Protein Biosynthesis</subject><subject>protein synthesis</subject><subject>Protein Synthesis Inhibitors - pharmacology</subject><subject>Proteomics</subject><subject>Proteomics - methods</subject><subject>Rhamnose - analogs & derivatives</subject><subject>Rhamnose - pharmacology</subject><subject>ribosomal RNA</subject><subject>ribosomes</subject><subject>Staphylococcal Infections - drug therapy</subject><subject>Staphylococcal Infections - metabolism</subject><subject>Staphylococcal Infections - microbiology</subject><subject>Staphylococcus aureus</subject><subject>stereoisomers</subject><subject>translation (genetics)</subject><issn>1874-3919</issn><issn>1876-7737</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kdtu1DAQhiMEogd4AiSUy61ULz4kzvoCpGrFSSyq1JZryxnPEq-ydrCTSnsHz8Qb8SR4u6WCG25sa-aff2b8FcULRueMMvlqM98MMYxzTpnKEVEL9ag4ZotGkqYRzeO7d0WEYuqoOElpQ6lkjWqeFkeCSa5UvTguftx0WBo_OvL56vqihLAdwuRtKcglMf3QGbIiM_7r-89zkQ9iHRkIhGlrYtj1Z7EzWx-Ss1jOPi2vzkrnO9e6MZX7ydD5Mu382GFyKafK69EM3a4PEACmVJop4pSeFU_Wpk_4_P4-Lb68e3uz_EBWl-8_Li9WBCrFRwJYtyjbtuYULEgqTd64oi3Y9aI2phU1t4IZDmpBkaEVojZNC7KWCgE5F6fFm4PvMLVbtIB-jKbXQ3R5mZ0Oxul_M951-mu41Q1lVS1ZNpjdG8TwbcI06q1LgH1vPIYpaV4JVVWUcZWl4iCFGFKKuH5ow6jew9MbfQdP7-HpA7xc9fLvCR9q_tDKgtcHAeZ_unUYdQKHHtC6iDBqG9x_G_wG9QewdA</recordid><startdate>20200106</startdate><enddate>20200106</enddate><creator>Carruthers, Nicholas J.</creator><creator>Stemmer, Paul M.</creator><creator>Media, Joe</creator><creator>Swartz, Ken</creator><creator>Wang, Xiaojuan</creator><creator>Aube, Nicholas</creator><creator>Hamann, Mark T.</creator><creator>Valeriote, Frederick</creator><creator>Shaw, Jiajiu</creator><general>Elsevier B.V</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>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20200106</creationdate><title>The anti-MRSA compound 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) inhibits protein synthesis in Staphylococcus aureus</title><author>Carruthers, Nicholas J. ; Stemmer, Paul M. ; Media, Joe ; Swartz, Ken ; Wang, Xiaojuan ; Aube, Nicholas ; Hamann, Mark T. ; Valeriote, Frederick ; Shaw, Jiajiu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-ce5be6bb520cdc606a03540bcdf85aab352d31a2c980e1ed335a7bc6569ece223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside</topic><topic>aminoacyl tRNA ligases</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>antibiotic resistance</topic><topic>Bacterial Proteins - metabolism</topic><topic>enzyme activity</topic><topic>hospitals</topic><topic>Humans</topic><topic>in vitro studies</topic><topic>inhibitory concentration 50</topic><topic>Kaempferols - pharmacology</topic><topic>KCR</topic><topic>luciferase</topic><topic>mass spectrometry</topic><topic>Mechanism of action</topic><topic>methicillin</topic><topic>Methicillin-resistant</topic><topic>methicillin-resistant Staphylococcus aureus</topic><topic>Methicillin-Resistant Staphylococcus aureus - drug effects</topic><topic>Methicillin-Resistant Staphylococcus aureus - isolation & purification</topic><topic>Methicillin-Resistant Staphylococcus aureus - metabolism</topic><topic>Microbial Sensitivity Tests - methods</topic><topic>mortality</topic><topic>oxacillin</topic><topic>patients</topic><topic>Protein Biosynthesis</topic><topic>protein synthesis</topic><topic>Protein Synthesis Inhibitors - pharmacology</topic><topic>Proteomics</topic><topic>Proteomics - methods</topic><topic>Rhamnose - analogs & derivatives</topic><topic>Rhamnose - pharmacology</topic><topic>ribosomal RNA</topic><topic>ribosomes</topic><topic>Staphylococcal Infections - drug therapy</topic><topic>Staphylococcal Infections - metabolism</topic><topic>Staphylococcal Infections - microbiology</topic><topic>Staphylococcus aureus</topic><topic>stereoisomers</topic><topic>translation (genetics)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carruthers, Nicholas J.</creatorcontrib><creatorcontrib>Stemmer, Paul M.</creatorcontrib><creatorcontrib>Media, Joe</creatorcontrib><creatorcontrib>Swartz, Ken</creatorcontrib><creatorcontrib>Wang, Xiaojuan</creatorcontrib><creatorcontrib>Aube, Nicholas</creatorcontrib><creatorcontrib>Hamann, Mark T.</creatorcontrib><creatorcontrib>Valeriote, Frederick</creatorcontrib><creatorcontrib>Shaw, Jiajiu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of proteomics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carruthers, Nicholas J.</au><au>Stemmer, Paul M.</au><au>Media, Joe</au><au>Swartz, Ken</au><au>Wang, Xiaojuan</au><au>Aube, Nicholas</au><au>Hamann, Mark T.</au><au>Valeriote, Frederick</au><au>Shaw, Jiajiu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The anti-MRSA compound 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) inhibits protein synthesis in Staphylococcus aureus</atitle><jtitle>Journal of proteomics</jtitle><addtitle>J Proteomics</addtitle><date>2020-01-06</date><risdate>2020</risdate><volume>210</volume><spage>103539</spage><epage>103539</epage><pages>103539-103539</pages><artnum>103539</artnum><issn>1874-3919</issn><eissn>1876-7737</eissn><abstract>Methicillin-resistant S aureus (MRSA) contributes to patient mortality and extended hospital stays. 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) is a natural product antibiotic that is effective against MRSA but has no known mechanism of action (MOA). We used proteomics to identify the MOA for KCR.
Methicillin sensitive S aureus and a mixture of four KCR stereoisomers were tested. A time-kill assay was used to choose a 4 h treatment using KCR at 5× its MIC for proteomic analysis. S aureus was treated in triplicate with KCR, oxacillin or vehicle and quantitative proteomic analysis was carried out using isobaric tags and mass spectrometry. 1190 proteins were identified and 552 were affected by KCR (q < 0.01). Ontology analysis identified 6 distinct translation-related categories that were affected by KCR (PIANO, 10% false-discovery rate) including structural constituent of ribosome, translation, rRNA binding, tRNA binding, tRNA processing and aminoacyl-tRNA ligase activity. Median fold changes (KCR vs Control) for small and large ribosomal components were 1.46 and 1.43 respectively. KCR inhibited the production of luciferase protein in an in vitro assay (IC50 39.6 μg/ml).
Upregulation of translation-related proteins in response to KCR indicates that KCR acts to disrupt S aureus protein synthesis. This was confirmed with an in vitro transcription/translation assay.
Methicillin-resistant S aureus (MRSA) contributes to patient mortality and extended hospital stays. 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) is a natural product antibiotic that is effective against MRSA but has no known mechanism of action (MOA). Using proteomic analysis we determined that KCR acts by inhibiting protein synthesis. KCR is an exciting novel antibiotic and this work represents an important step in its development towards clinical use.
[Display omitted]
•A mixture of KCR isomers ZZ, EZ, ZE and EE was tested for antimicrobial activity against methicillin-sensitive S aureus.•Translation-associated proteins were increased after KCR treatment suggesting that KCR acts to inhibit translation.•An in vitro translation assay supported the proposed mechanism.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>31629958</pmid><doi>10.1016/j.jprot.2019.103539</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside aminoacyl tRNA ligases Anti-Bacterial Agents - pharmacology antibiotic resistance Bacterial Proteins - metabolism enzyme activity hospitals Humans in vitro studies inhibitory concentration 50 Kaempferols - pharmacology KCR luciferase mass spectrometry Mechanism of action methicillin Methicillin-resistant methicillin-resistant Staphylococcus aureus Methicillin-Resistant Staphylococcus aureus - drug effects Methicillin-Resistant Staphylococcus aureus - isolation & purification Methicillin-Resistant Staphylococcus aureus - metabolism Microbial Sensitivity Tests - methods mortality oxacillin patients Protein Biosynthesis protein synthesis Protein Synthesis Inhibitors - pharmacology Proteomics Proteomics - methods Rhamnose - analogs & derivatives Rhamnose - pharmacology ribosomal RNA ribosomes Staphylococcal Infections - drug therapy Staphylococcal Infections - metabolism Staphylococcal Infections - microbiology Staphylococcus aureus stereoisomers translation (genetics) |
| title | The anti-MRSA compound 3-O-alpha-L-(2″,3″-di-p-coumaroyl)rhamnoside (KCR) inhibits protein synthesis in Staphylococcus aureus |
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