Initial Binding Sites of Antimicrobial Peptides in Staphylococcus aureus and Escherichia coli
We examined the initial binding sites of magainin 1, cecropin P1 and lactoferricin B in Staphylococcus aureus and Escherichia coli. All 3 peptides were active against E. coli, whereas only lactoferricin B exerted any activity against S. aureus. Soluble lipoteichoic acid and lipopolysaccharide both i...
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| Veröffentlicht in: | Scandinavian journal of infectious diseases 1999, Vol.31 (5), p.467-473 |
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| container_title | Scandinavian journal of infectious diseases |
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| creator | Vorland, L H Ulvatne, H Rekdal, O Svendsen, J S |
| description | We examined the initial binding sites of magainin 1, cecropin P1 and lactoferricin B in Staphylococcus aureus and Escherichia coli. All 3 peptides were active against E. coli, whereas only lactoferricin B exerted any activity against S. aureus. Soluble lipoteichoic acid and lipopolysaccharide both interacted with all 3 peptides, whereas soluble teichoic acid interacted with lactoferricin B only. Antibodies against teichoic acid diminished the activity of lactoferricin B, while antibodies against lipoteichoic acid had no influence on the activity of lactoferricin B. Antibodies against lipopolysaccharide diminished the activity of lactoferricin B and magainin 1, but had no effect on the activity of cecropin P1 against E. coli. We conclude that the initial binding sites of lactoferricin B in S. aureus, and of lactoferricin B and magainin 1 in E. coli, are teichoic acid and lipopolysaccharide, respectively. Cecropin P1 seems to interact with a different binding site than those of magainin 1 and lactoferricin B in E. coli. |
| doi_str_mv | 10.1080/00365549950163987 |
| format | Article |
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All 3 peptides were active against E. coli, whereas only lactoferricin B exerted any activity against S. aureus. Soluble lipoteichoic acid and lipopolysaccharide both interacted with all 3 peptides, whereas soluble teichoic acid interacted with lactoferricin B only. Antibodies against teichoic acid diminished the activity of lactoferricin B, while antibodies against lipoteichoic acid had no influence on the activity of lactoferricin B. Antibodies against lipopolysaccharide diminished the activity of lactoferricin B and magainin 1, but had no effect on the activity of cecropin P1 against E. coli. We conclude that the initial binding sites of lactoferricin B in S. aureus, and of lactoferricin B and magainin 1 in E. coli, are teichoic acid and lipopolysaccharide, respectively. Cecropin P1 seems to interact with a different binding site than those of magainin 1 and lactoferricin B in E. coli.</description><identifier>ISSN: 0036-5548</identifier><identifier>EISSN: 1651-1980</identifier><identifier>DOI: 10.1080/00365549950163987</identifier><identifier>PMID: 10576125</identifier><identifier>CODEN: SJIDB7</identifier><language>eng</language><publisher>Basingstoke: Informa UK Ltd</publisher><subject>Anti-Bacterial Agents - metabolism ; Antibacterial agents ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antibodies, Bacterial - immunology ; Antimicrobial Cationic Peptides ; Binding Sites - drug effects ; Binding, Competitive ; Biological and medical sciences ; Cecropin P1 ; Drug Interactions ; Escherichia coli ; Escherichia coli - metabolism ; lactoferricin B ; Lactoferrin - analogs & derivatives ; Lactoferrin - metabolism ; lipopolysaccharides ; Lipopolysaccharides - immunology ; Lipopolysaccharides - pharmacology ; magainin I ; Medical sciences ; Microbial Sensitivity Tests ; Peptides - metabolism ; Pharmacology. Drug treatments ; Staphylococcus aureus ; Staphylococcus aureus - metabolism ; teichoic acids ; Teichoic Acids - immunology ; Teichoic Acids - pharmacology ; Xenopus Proteins</subject><ispartof>Scandinavian journal of infectious diseases, 1999, Vol.31 (5), p.467-473</ispartof><rights>1999 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted 1999</rights><rights>2000 INIST-CNRS</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-353437123adf0fd85131ff683cb562a1d2a96022a92d7125bc57d62c8c86ad533</citedby><cites>FETCH-LOGICAL-c462t-353437123adf0fd85131ff683cb562a1d2a96022a92d7125bc57d62c8c86ad533</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.1080/00365549950163987$$EPDF$$P50$$Ginformahealthcare$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.1080/00365549950163987$$EHTML$$P50$$Ginformahealthcare$$H</linktohtml><link.rule.ids>314,780,784,4021,27921,27922,27923,59645,59751,60434,60540,61219,61254,61400,61435</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1188969$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10576125$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vorland, L H</creatorcontrib><creatorcontrib>Ulvatne, H</creatorcontrib><creatorcontrib>Rekdal, O</creatorcontrib><creatorcontrib>Svendsen, J S</creatorcontrib><title>Initial Binding Sites of Antimicrobial Peptides in Staphylococcus aureus and Escherichia coli</title><title>Scandinavian journal of infectious diseases</title><addtitle>Scand J Infect Dis</addtitle><description>We examined the initial binding sites of magainin 1, cecropin P1 and lactoferricin B in Staphylococcus aureus and Escherichia coli. All 3 peptides were active against E. coli, whereas only lactoferricin B exerted any activity against S. aureus. Soluble lipoteichoic acid and lipopolysaccharide both interacted with all 3 peptides, whereas soluble teichoic acid interacted with lactoferricin B only. Antibodies against teichoic acid diminished the activity of lactoferricin B, while antibodies against lipoteichoic acid had no influence on the activity of lactoferricin B. Antibodies against lipopolysaccharide diminished the activity of lactoferricin B and magainin 1, but had no effect on the activity of cecropin P1 against E. coli. We conclude that the initial binding sites of lactoferricin B in S. aureus, and of lactoferricin B and magainin 1 in E. coli, are teichoic acid and lipopolysaccharide, respectively. Cecropin P1 seems to interact with a different binding site than those of magainin 1 and lactoferricin B in E. coli.</description><subject>Anti-Bacterial Agents - metabolism</subject><subject>Antibacterial agents</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antibodies, Bacterial - immunology</subject><subject>Antimicrobial Cationic Peptides</subject><subject>Binding Sites - drug effects</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Cecropin P1</subject><subject>Drug Interactions</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>lactoferricin B</subject><subject>Lactoferrin - analogs & derivatives</subject><subject>Lactoferrin - metabolism</subject><subject>lipopolysaccharides</subject><subject>Lipopolysaccharides - immunology</subject><subject>Lipopolysaccharides - pharmacology</subject><subject>magainin I</subject><subject>Medical sciences</subject><subject>Microbial Sensitivity Tests</subject><subject>Peptides - metabolism</subject><subject>Pharmacology. Drug treatments</subject><subject>Staphylococcus aureus</subject><subject>Staphylococcus aureus - metabolism</subject><subject>teichoic acids</subject><subject>Teichoic Acids - immunology</subject><subject>Teichoic Acids - pharmacology</subject><subject>Xenopus Proteins</subject><issn>0036-5548</issn><issn>1651-1980</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1rFTEUhoNY7LX6A9zILMTd2JzJTSaDbtpStVBoobqU4dx8OCmZ5JpkkP57c7lXVIRuchbv8x5yHkJeAX0HVNJTSpngfD0MnIJgg-yfkBUIDi0Mkj4lq13eVkAek-c531NK14LRZ-QYKO8FdHxFvl0FVxz65twF7cL35s4Vk5tom7NQ3OxUiptdfGu2xemauNDcFdxODz6qqNSSG1yS2Y2gm8usJpOcmhw2Knr3ghxZ9Nm8PMwT8vXj5ZeLz-31zaeri7PrVq1FV1rG2Zr10DHUllotOTCwVkimNlx0CLrDQdCuvp2uGN8o3mvRKamkQM0ZOyFv93u3Kf5YTC7j7LIy3mMwcckj9IIOnEEFYQ_Wu3JOxo7b5GZMDyPQced0_M9p7bw-LF82s9F_NfYSK_DmAGBW6G3CoFz-w4GUgxgq9mGPuWBjmvFnTF6PBavJ9LvDHvvG-3_qk0FfJoXJjPdxSaH6feSIX2dSo0Q</recordid><startdate>1999</startdate><enddate>1999</enddate><creator>Vorland, L H</creator><creator>Ulvatne, H</creator><creator>Rekdal, O</creator><creator>Svendsen, J S</creator><general>Informa UK Ltd</general><general>Taylor & Francis</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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>1999</creationdate><title>Initial Binding Sites of Antimicrobial Peptides in Staphylococcus aureus and Escherichia coli</title><author>Vorland, L H ; Ulvatne, H ; Rekdal, O ; Svendsen, J S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-353437123adf0fd85131ff683cb562a1d2a96022a92d7125bc57d62c8c86ad533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Anti-Bacterial Agents - metabolism</topic><topic>Antibacterial agents</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Antibodies, Bacterial - immunology</topic><topic>Antimicrobial Cationic Peptides</topic><topic>Binding Sites - drug effects</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Cecropin P1</topic><topic>Drug Interactions</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>lactoferricin B</topic><topic>Lactoferrin - analogs & derivatives</topic><topic>Lactoferrin - metabolism</topic><topic>lipopolysaccharides</topic><topic>Lipopolysaccharides - immunology</topic><topic>Lipopolysaccharides - pharmacology</topic><topic>magainin I</topic><topic>Medical sciences</topic><topic>Microbial Sensitivity Tests</topic><topic>Peptides - metabolism</topic><topic>Pharmacology. Drug treatments</topic><topic>Staphylococcus aureus</topic><topic>Staphylococcus aureus - metabolism</topic><topic>teichoic acids</topic><topic>Teichoic Acids - immunology</topic><topic>Teichoic Acids - pharmacology</topic><topic>Xenopus Proteins</topic><toplevel>online_resources</toplevel><creatorcontrib>Vorland, L H</creatorcontrib><creatorcontrib>Ulvatne, H</creatorcontrib><creatorcontrib>Rekdal, O</creatorcontrib><creatorcontrib>Svendsen, J S</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>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><jtitle>Scandinavian journal of infectious diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vorland, L H</au><au>Ulvatne, H</au><au>Rekdal, O</au><au>Svendsen, J S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Initial Binding Sites of Antimicrobial Peptides in Staphylococcus aureus and Escherichia coli</atitle><jtitle>Scandinavian journal of infectious diseases</jtitle><addtitle>Scand J Infect Dis</addtitle><date>1999</date><risdate>1999</risdate><volume>31</volume><issue>5</issue><spage>467</spage><epage>473</epage><pages>467-473</pages><issn>0036-5548</issn><eissn>1651-1980</eissn><coden>SJIDB7</coden><abstract>We examined the initial binding sites of magainin 1, cecropin P1 and lactoferricin B in Staphylococcus aureus and Escherichia coli. All 3 peptides were active against E. coli, whereas only lactoferricin B exerted any activity against S. aureus. Soluble lipoteichoic acid and lipopolysaccharide both interacted with all 3 peptides, whereas soluble teichoic acid interacted with lactoferricin B only. Antibodies against teichoic acid diminished the activity of lactoferricin B, while antibodies against lipoteichoic acid had no influence on the activity of lactoferricin B. Antibodies against lipopolysaccharide diminished the activity of lactoferricin B and magainin 1, but had no effect on the activity of cecropin P1 against E. coli. We conclude that the initial binding sites of lactoferricin B in S. aureus, and of lactoferricin B and magainin 1 in E. coli, are teichoic acid and lipopolysaccharide, respectively. Cecropin P1 seems to interact with a different binding site than those of magainin 1 and lactoferricin B in E. coli.</abstract><cop>Basingstoke</cop><pub>Informa UK Ltd</pub><pmid>10576125</pmid><doi>10.1080/00365549950163987</doi><tpages>7</tpages></addata></record> |
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| ispartof | Scandinavian journal of infectious diseases, 1999, Vol.31 (5), p.467-473 |
| issn | 0036-5548 1651-1980 |
| language | eng |
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| source | MEDLINE; Taylor & Francis CRKN Medical; Taylor & Francis:Master (3349 titles) |
| subjects | Anti-Bacterial Agents - metabolism Antibacterial agents Antibiotics. Antiinfectious agents. Antiparasitic agents Antibodies, Bacterial - immunology Antimicrobial Cationic Peptides Binding Sites - drug effects Binding, Competitive Biological and medical sciences Cecropin P1 Drug Interactions Escherichia coli Escherichia coli - metabolism lactoferricin B Lactoferrin - analogs & derivatives Lactoferrin - metabolism lipopolysaccharides Lipopolysaccharides - immunology Lipopolysaccharides - pharmacology magainin I Medical sciences Microbial Sensitivity Tests Peptides - metabolism Pharmacology. Drug treatments Staphylococcus aureus Staphylococcus aureus - metabolism teichoic acids Teichoic Acids - immunology Teichoic Acids - pharmacology Xenopus Proteins |
| title | Initial Binding Sites of Antimicrobial Peptides in Staphylococcus aureus and Escherichia coli |
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