The beta-lactam-resistance modifier (-)-epicatechin gallate alters the architecture of the cell wall of Staphylococcus aureus
1 Microbiology Group, School of Pharmacy, 29–39 Brunswick Square, London WC1N 1AX, UK 2 Bayer Healthcare AG, Pharma Research Center, D-42096 Wuppertal, Germany 3 Mitsui Norin Co. Ltd, 1-2-9 Nishi-Shinbashi, Minato-Ku, Tokyo 105-8427, Japan Correspondence Peter W. Taylor peter.taylor{at}pharmacy.ac.u...
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The beta-lactam-resistance modifier (-)-epicatechin gallate alters the architecture of the cell wall of Staphylococcus aureus |
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Stapleton, Paul D Shah, Saroj Ehlert, Kerstin Hara, Yukihiko Taylor, Peter W |
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beta-Lactam Resistance - drug effects beta-Lactam Resistance - physiology Biological and medical sciences Catechin - analogs & derivatives Catechin - chemistry Catechin - pharmacology Cell Wall - chemistry Cell Wall - drug effects Cell Wall - enzymology Fundamental and applied biological sciences. Psychology Microbiology Penicillin-Binding Proteins Peptidoglycan - metabolism Staphylococcus aureus Staphylococcus aureus - drug effects Staphylococcus aureus - genetics Staphylococcus aureus - growth & development |
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Microbiology (Society for General Microbiology), 2007-07, Vol.153 (7), p.2093-2103 |
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1 Microbiology Group, School of Pharmacy, 29–39 Brunswick Square, London WC1N 1AX, UK
2 Bayer Healthcare AG, Pharma Research Center, D-42096 Wuppertal, Germany
3 Mitsui Norin Co. Ltd, 1-2-9 Nishi-Shinbashi, Minato-Ku, Tokyo 105-8427, Japan
Correspondence Peter W. Taylor peter.taylor{at}pharmacy.ac.uk
(–)-Epicatechin gallate (ECg), a component of green tea, sensitizes meticillin-resistant Staphylococcus aureus (MRSA) to β -lactam antibiotics, promotes staphylococcal cell aggregation and increases cell-wall thickness. The potentiation of β -lactam activity against MRSA by ECg was not due to decreased bacterial penicillin-binding protein (PBP) 2a expression or ECg binding to peptidoglycan. A 5–10 % reduction in peptidoglycan cross-linking was observed. Reduced cross-linking was insufficient to compromise the integrity of the cell wall and no evidence of PBP2a activity was detected in the muropeptide composition of ECg-grown cells. ECg increased the quantity of autolysins associated with the cell wall, even though the cells were less susceptible to Triton X-100-induced autolysis than cells grown in the absence of ECg. ECg promoted increased lysostaphin resistance that was not due to alteration of the pentaglycine cross-bridge configuration or inhibition of lysostaphin activity. Rather, decreased lysostaphin susceptibility was associated with structural changes to wall teichoic acid (WTA), an acid-labile component of peptidoglycan. ECg also promoted lipoteichoic acid (LTA) release from the cytoplasmic membrane. It is proposed that ECg reduces β -lactam resistance in MRSA either by binding to PBPs at sites distinct from the penicillin-binding site or by intercalation into the cytoplasmic membrane, displacing LTA from the phospholipid palisade. Thus, ECg-mediated alterations to the physical nature of the bilayer will elicit structural changes to WTA that result in modulation of the cell-surface properties necessary to maintain the β -lactam-resistant phenotype.
Abbreviations: EC, (–)-epicatechin; ECg, (–)-epicatechin gallate; EGCg, (–)-epigallocatechin gallate; LTA, lipoteichoic acid; MRSA, meticillin-resistant Staphylococcus aureus ; MSSA, meticillin-susceptible S. aureus ; PBP, penicillin-binding protein; VISA, vancomycin-intermediate-resistant S. aureus ; WTA, wall teichoic acid |
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2 Bayer Healthcare AG, Pharma Research Center, D-42096 Wuppertal, Germany
3 Mitsui Norin Co. Ltd, 1-2-9 Nishi-Shinbashi, Minato-Ku, Tokyo 105-8427, Japan
Correspondence Peter W. Taylor peter.taylor{at}pharmacy.ac.uk
(–)-Epicatechin gallate (ECg), a component of green tea, sensitizes meticillin-resistant Staphylococcus aureus (MRSA) to β -lactam antibiotics, promotes staphylococcal cell aggregation and increases cell-wall thickness. The potentiation of β -lactam activity against MRSA by ECg was not due to decreased bacterial penicillin-binding protein (PBP) 2a expression or ECg binding to peptidoglycan. A 5–10 % reduction in peptidoglycan cross-linking was observed. Reduced cross-linking was insufficient to compromise the integrity of the cell wall and no evidence of PBP2a activity was detected in the muropeptide composition of ECg-grown cells. ECg increased the quantity of autolysins associated with the cell wall, even though the cells were less susceptible to Triton X-100-induced autolysis than cells grown in the absence of ECg. ECg promoted increased lysostaphin resistance that was not due to alteration of the pentaglycine cross-bridge configuration or inhibition of lysostaphin activity. Rather, decreased lysostaphin susceptibility was associated with structural changes to wall teichoic acid (WTA), an acid-labile component of peptidoglycan. ECg also promoted lipoteichoic acid (LTA) release from the cytoplasmic membrane. It is proposed that ECg reduces β -lactam resistance in MRSA either by binding to PBPs at sites distinct from the penicillin-binding site or by intercalation into the cytoplasmic membrane, displacing LTA from the phospholipid palisade. Thus, ECg-mediated alterations to the physical nature of the bilayer will elicit structural changes to WTA that result in modulation of the cell-surface properties necessary to maintain the β -lactam-resistant phenotype.
Abbreviations: EC, (–)-epicatechin; ECg, (–)-epicatechin gallate; EGCg, (–)-epigallocatechin gallate; LTA, lipoteichoic acid; MRSA, meticillin-resistant Staphylococcus aureus ; MSSA, meticillin-susceptible S. aureus ; PBP, penicillin-binding protein; VISA, vancomycin-intermediate-resistant S. aureus ; WTA, wall teichoic acid</description><identifier>ISSN: 1350-0872</identifier><identifier>EISSN: 1465-2080</identifier><identifier>DOI: 10.1099/mic.0.2007/007807-0</identifier><identifier>PMID: 17600054</identifier><language>eng</language><publisher>Reading: Soc General Microbiol</publisher><subject>beta-Lactam Resistance - drug effects ; beta-Lactam Resistance - physiology ; Biological and medical sciences ; Catechin - analogs & derivatives ; Catechin - chemistry ; Catechin - pharmacology ; Cell Wall - chemistry ; Cell Wall - drug effects ; Cell Wall - enzymology ; Fundamental and applied biological sciences. Psychology ; Microbiology ; Penicillin-Binding Proteins ; Peptidoglycan - metabolism ; Staphylococcus aureus ; Staphylococcus aureus - drug effects ; Staphylococcus aureus - genetics ; Staphylococcus aureus - growth & development</subject><ispartof>Microbiology (Society for General Microbiology), 2007-07, Vol.153 (7), p.2093-2103</ispartof><rights>2008 INIST-CNRS</rights><rights>2007 SGM 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c428t-285a589c48246c39789d6ec163f3290b3ef9d06f991e8c7e01edeae71922f8c93</citedby><cites>FETCH-LOGICAL-c428t-285a589c48246c39789d6ec163f3290b3ef9d06f991e8c7e01edeae71922f8c93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063568/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063568/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,734,787,791,892,27985,27986,54176,54178</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18907050$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17600054$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stapleton, Paul D</creatorcontrib><creatorcontrib>Shah, Saroj</creatorcontrib><creatorcontrib>Ehlert, Kerstin</creatorcontrib><creatorcontrib>Hara, Yukihiko</creatorcontrib><creatorcontrib>Taylor, Peter W</creatorcontrib><title>The beta-lactam-resistance modifier (-)-epicatechin gallate alters the architecture of the cell wall of Staphylococcus aureus</title><title>Microbiology (Society for General Microbiology)</title><addtitle>Microbiology (Reading)</addtitle><description>1 Microbiology Group, School of Pharmacy, 29–39 Brunswick Square, London WC1N 1AX, UK
2 Bayer Healthcare AG, Pharma Research Center, D-42096 Wuppertal, Germany
3 Mitsui Norin Co. Ltd, 1-2-9 Nishi-Shinbashi, Minato-Ku, Tokyo 105-8427, Japan
Correspondence Peter W. Taylor peter.taylor{at}pharmacy.ac.uk
(–)-Epicatechin gallate (ECg), a component of green tea, sensitizes meticillin-resistant Staphylococcus aureus (MRSA) to β -lactam antibiotics, promotes staphylococcal cell aggregation and increases cell-wall thickness. The potentiation of β -lactam activity against MRSA by ECg was not due to decreased bacterial penicillin-binding protein (PBP) 2a expression or ECg binding to peptidoglycan. A 5–10 % reduction in peptidoglycan cross-linking was observed. Reduced cross-linking was insufficient to compromise the integrity of the cell wall and no evidence of PBP2a activity was detected in the muropeptide composition of ECg-grown cells. ECg increased the quantity of autolysins associated with the cell wall, even though the cells were less susceptible to Triton X-100-induced autolysis than cells grown in the absence of ECg. ECg promoted increased lysostaphin resistance that was not due to alteration of the pentaglycine cross-bridge configuration or inhibition of lysostaphin activity. Rather, decreased lysostaphin susceptibility was associated with structural changes to wall teichoic acid (WTA), an acid-labile component of peptidoglycan. ECg also promoted lipoteichoic acid (LTA) release from the cytoplasmic membrane. It is proposed that ECg reduces β -lactam resistance in MRSA either by binding to PBPs at sites distinct from the penicillin-binding site or by intercalation into the cytoplasmic membrane, displacing LTA from the phospholipid palisade. Thus, ECg-mediated alterations to the physical nature of the bilayer will elicit structural changes to WTA that result in modulation of the cell-surface properties necessary to maintain the β -lactam-resistant phenotype.
Abbreviations: EC, (–)-epicatechin; ECg, (–)-epicatechin gallate; EGCg, (–)-epigallocatechin gallate; LTA, lipoteichoic acid; MRSA, meticillin-resistant Staphylococcus aureus ; MSSA, meticillin-susceptible S. aureus ; PBP, penicillin-binding protein; VISA, vancomycin-intermediate-resistant S. aureus ; WTA, wall teichoic acid</description><subject>beta-Lactam Resistance - drug effects</subject><subject>beta-Lactam Resistance - physiology</subject><subject>Biological and medical sciences</subject><subject>Catechin - analogs & derivatives</subject><subject>Catechin - chemistry</subject><subject>Catechin - pharmacology</subject><subject>Cell Wall - chemistry</subject><subject>Cell Wall - drug effects</subject><subject>Cell Wall - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microbiology</subject><subject>Penicillin-Binding Proteins</subject><subject>Peptidoglycan - metabolism</subject><subject>Staphylococcus aureus</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Staphylococcus aureus - genetics</subject><subject>Staphylococcus aureus - growth & development</subject><issn>1350-0872</issn><issn>1465-2080</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqFkUtv1TAQhSMEog_4BUgoG1C78O3YTvzYIKGKl1SJBWVt-TqTG6MkvtgOVRf8dxzuFYUVC8vWnG_OeHSq6gWFDQWtrybvNrBhAPKqHAWSwKPqlDaiJQwUPC5v3gIBJdlJdZbSN4AiAn1anVApAKBtTquftwPWW8yWjNZlO5GIyadsZ4f1FDrfe4z1BbkkuPfOZnSDn-udHcfyru2YMaY6Fwsbi1LkvESsQ_-75nAc67vCroUv2e6H-zG44NySalu4JT2rnvR2TPj8eJ9XX9-_u73-SG4-f_h0_faGuIapTJhqbau0axRrhONaKt0JdFTwnjMNW4697kD0WlNUTiJQ7NCipJqxXjnNz6s3B9_9sp2wczjnaEezj36y8d4E682_yuwHsws_DAPBW6GKweujQQzfF0zZTD6t-9kZw5KMBNFKqZv_giWZhrdKFJAfQBdDShH7P7-hYNZ8S6MzYNZ8zSFfA6Xr5d-LPPQcAy3AqyNgk7NjH0uSPj1wSoOEdjW6PHCD3w13PqLZ4VwmxrD1YR1NW25kma45_wVHt782</recordid><startdate>20070701</startdate><enddate>20070701</enddate><creator>Stapleton, Paul D</creator><creator>Shah, Saroj</creator><creator>Ehlert, Kerstin</creator><creator>Hara, Yukihiko</creator><creator>Taylor, Peter W</creator><general>Soc General Microbiol</general><general>Society for General Microbiology</general><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>C1K</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070701</creationdate><title>The beta-lactam-resistance modifier (-)-epicatechin gallate alters the architecture of the cell wall of Staphylococcus aureus</title><author>Stapleton, Paul D ; Shah, Saroj ; Ehlert, Kerstin ; Hara, Yukihiko ; Taylor, Peter W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c428t-285a589c48246c39789d6ec163f3290b3ef9d06f991e8c7e01edeae71922f8c93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>beta-Lactam Resistance - drug effects</topic><topic>beta-Lactam Resistance - physiology</topic><topic>Biological and medical sciences</topic><topic>Catechin - analogs & derivatives</topic><topic>Catechin - chemistry</topic><topic>Catechin - pharmacology</topic><topic>Cell Wall - chemistry</topic><topic>Cell Wall - drug effects</topic><topic>Cell Wall - enzymology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microbiology</topic><topic>Penicillin-Binding Proteins</topic><topic>Peptidoglycan - metabolism</topic><topic>Staphylococcus aureus</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Staphylococcus aureus - genetics</topic><topic>Staphylococcus aureus - growth & development</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stapleton, Paul D</creatorcontrib><creatorcontrib>Shah, Saroj</creatorcontrib><creatorcontrib>Ehlert, Kerstin</creatorcontrib><creatorcontrib>Hara, Yukihiko</creatorcontrib><creatorcontrib>Taylor, Peter W</creatorcontrib><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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Microbiology (Society for General Microbiology)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stapleton, Paul D</au><au>Shah, Saroj</au><au>Ehlert, Kerstin</au><au>Hara, Yukihiko</au><au>Taylor, Peter W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The beta-lactam-resistance modifier (-)-epicatechin gallate alters the architecture of the cell wall of Staphylococcus aureus</atitle><jtitle>Microbiology (Society for General Microbiology)</jtitle><addtitle>Microbiology (Reading)</addtitle><date>2007-07-01</date><risdate>2007</risdate><volume>153</volume><issue>7</issue><spage>2093</spage><epage>2103</epage><pages>2093-2103</pages><issn>1350-0872</issn><eissn>1465-2080</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>1 Microbiology Group, School of Pharmacy, 29–39 Brunswick Square, London WC1N 1AX, UK
2 Bayer Healthcare AG, Pharma Research Center, D-42096 Wuppertal, Germany
3 Mitsui Norin Co. Ltd, 1-2-9 Nishi-Shinbashi, Minato-Ku, Tokyo 105-8427, Japan
Correspondence Peter W. Taylor peter.taylor{at}pharmacy.ac.uk
(–)-Epicatechin gallate (ECg), a component of green tea, sensitizes meticillin-resistant Staphylococcus aureus (MRSA) to β -lactam antibiotics, promotes staphylococcal cell aggregation and increases cell-wall thickness. The potentiation of β -lactam activity against MRSA by ECg was not due to decreased bacterial penicillin-binding protein (PBP) 2a expression or ECg binding to peptidoglycan. A 5–10 % reduction in peptidoglycan cross-linking was observed. Reduced cross-linking was insufficient to compromise the integrity of the cell wall and no evidence of PBP2a activity was detected in the muropeptide composition of ECg-grown cells. ECg increased the quantity of autolysins associated with the cell wall, even though the cells were less susceptible to Triton X-100-induced autolysis than cells grown in the absence of ECg. ECg promoted increased lysostaphin resistance that was not due to alteration of the pentaglycine cross-bridge configuration or inhibition of lysostaphin activity. Rather, decreased lysostaphin susceptibility was associated with structural changes to wall teichoic acid (WTA), an acid-labile component of peptidoglycan. ECg also promoted lipoteichoic acid (LTA) release from the cytoplasmic membrane. It is proposed that ECg reduces β -lactam resistance in MRSA either by binding to PBPs at sites distinct from the penicillin-binding site or by intercalation into the cytoplasmic membrane, displacing LTA from the phospholipid palisade. Thus, ECg-mediated alterations to the physical nature of the bilayer will elicit structural changes to WTA that result in modulation of the cell-surface properties necessary to maintain the β -lactam-resistant phenotype.
Abbreviations: EC, (–)-epicatechin; ECg, (–)-epicatechin gallate; EGCg, (–)-epigallocatechin gallate; LTA, lipoteichoic acid; MRSA, meticillin-resistant Staphylococcus aureus ; MSSA, meticillin-susceptible S. aureus ; PBP, penicillin-binding protein; VISA, vancomycin-intermediate-resistant S. aureus ; WTA, wall teichoic acid</abstract><cop>Reading</cop><pub>Soc General Microbiol</pub><pmid>17600054</pmid><doi>10.1099/mic.0.2007/007807-0</doi><oa>free_for_read</oa></addata></record> |