The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm
The localization of immunolabelled antimicrobial peptides was studied using transmission electron microscopy. Staphylococcus aureus and Escherichia coli were exposed to lactoferricin B (17–41), lactoferricin B (17–31) and D-lactoferricin B (17–31). E. coli was also exposed to cecropin P1 and magaini...
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| Veröffentlicht in: | FEBS letters 2001-11, Vol.508 (3), p.389-393 |
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| creator | Haukland, H.H. Ulvatne, H. Sandvik, K. Vorland, L.H. |
| description | The localization of immunolabelled antimicrobial peptides was studied using transmission electron microscopy.
Staphylococcus aureus and
Escherichia coli were exposed to lactoferricin B (17–41), lactoferricin B (17–31) and
D-lactoferricin B (17–31).
E. coli was also exposed to cecropin P1 and magainin 2. The lactoferricins were found in the cytoplasm of both bacteria. In
S. aureus the amount of cytoplasmic lactoferricin B (17–41) was time- and concentration-dependent, reaching a maximum within 30 min. Cecropin P1 was confined to the cell wall, while magainin 2 was found in the cytoplasm of
E. coli. The finding of intracellularly localized magainin is not reported previously. |
| doi_str_mv | 10.1016/S0014-5793(01)03100-3 |
| format | Article |
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Staphylococcus aureus and
Escherichia coli were exposed to lactoferricin B (17–41), lactoferricin B (17–31) and
D-lactoferricin B (17–31).
E. coli was also exposed to cecropin P1 and magainin 2. The lactoferricins were found in the cytoplasm of both bacteria. In
S. aureus the amount of cytoplasmic lactoferricin B (17–41) was time- and concentration-dependent, reaching a maximum within 30 min. Cecropin P1 was confined to the cell wall, while magainin 2 was found in the cytoplasm of
E. coli. The finding of intracellularly localized magainin is not reported previously.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(01)03100-3</identifier><identifier>PMID: 11728458</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Antimicrobial Cationic Peptides - metabolism ; Antimicrobial Cationic Peptides - pharmacology ; Antimicrobial peptide ; BPW, Bacto peptone water ; Cec P1, cecropin P1 ; Cecropin ; Cell Membrane - metabolism ; CFU, colony-forming units ; Cytoplasm ; Cytoplasm - metabolism ; Cytoplasmic membrane ; Escherichia coli - drug effects ; Escherichia coli - metabolism ; Immunohistochemistry ; Lactoferricin ; Lactoferrin - analogs & derivatives ; Lactoferrin - metabolism ; Lactoferrin - pharmacology ; Lfcin B, bovine lactoferricin ; Mag 2, magainin 2 ; Magainin ; Magainins ; MBC, minimal bactericidal concentration ; MIC, minimal inhibitory concentration ; Microbial Sensitivity Tests ; Staphylococcus aureus - drug effects ; Staphylococcus aureus - metabolism ; TEM, transmission electron microscopy ; Xenopus Proteins</subject><ispartof>FEBS letters, 2001-11, Vol.508 (3), p.389-393</ispartof><rights>2001 Federation of European Biochemical Societies</rights><rights>FEBS Letters 508 (2001) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5523-6885811280026cb839ed3e21ebe2c860b76cf16b50d0c29d4f78a422268c61ad3</citedby><cites>FETCH-LOGICAL-c5523-6885811280026cb839ed3e21ebe2c860b76cf16b50d0c29d4f78a422268c61ad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2801%2903100-3$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579301031003$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27903,27904,45553,45554,46387,46811,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11728458$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haukland, H.H.</creatorcontrib><creatorcontrib>Ulvatne, H.</creatorcontrib><creatorcontrib>Sandvik, K.</creatorcontrib><creatorcontrib>Vorland, L.H.</creatorcontrib><title>The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The localization of immunolabelled antimicrobial peptides was studied using transmission electron microscopy.
Staphylococcus aureus and
Escherichia coli were exposed to lactoferricin B (17–41), lactoferricin B (17–31) and
D-lactoferricin B (17–31).
E. coli was also exposed to cecropin P1 and magainin 2. The lactoferricins were found in the cytoplasm of both bacteria. In
S. aureus the amount of cytoplasmic lactoferricin B (17–41) was time- and concentration-dependent, reaching a maximum within 30 min. Cecropin P1 was confined to the cell wall, while magainin 2 was found in the cytoplasm of
E. coli. The finding of intracellularly localized magainin is not reported previously.</description><subject>Antimicrobial Cationic Peptides - metabolism</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Antimicrobial peptide</subject><subject>BPW, Bacto peptone water</subject><subject>Cec P1, cecropin P1</subject><subject>Cecropin</subject><subject>Cell Membrane - metabolism</subject><subject>CFU, colony-forming units</subject><subject>Cytoplasm</subject><subject>Cytoplasm - metabolism</subject><subject>Cytoplasmic membrane</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - metabolism</subject><subject>Immunohistochemistry</subject><subject>Lactoferricin</subject><subject>Lactoferrin - analogs & derivatives</subject><subject>Lactoferrin - metabolism</subject><subject>Lactoferrin - pharmacology</subject><subject>Lfcin B, bovine lactoferricin</subject><subject>Mag 2, magainin 2</subject><subject>Magainin</subject><subject>Magainins</subject><subject>MBC, minimal bactericidal concentration</subject><subject>MIC, minimal inhibitory concentration</subject><subject>Microbial Sensitivity Tests</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Staphylococcus aureus - metabolism</subject><subject>TEM, transmission electron microscopy</subject><subject>Xenopus Proteins</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUtP3TAQha2qCC6Pn9DKq4ouAh47cZxVVRAvCYkFsLYce9K6yqt2LtVd88fr5F7RJV1Z4_nOmdEcQj4BOwMG8vyRMcizoqzEKYOvTABjmfhAVqBKkYlcqo9k9YYckMMYf7FUK6j2yQFAyVVeqBV5ffqJ1PST77wNQ-1NS0ccJ-8w0tbYaWgwBG99Ty8S5mhnfhjfp5LTxMdIhxcMdEomdaIxzAZ2Mw1ja2KypB12dTA9LuKAMRnTpJ4Fb9gx2WtMG_Fk9x6R5-urp8vb7P7h5u7y-31mi4KLTCpVKACuGOPS1kpU6ARywBq5VZLVpbQNyLpgjlleubwplck551JZCcaJI_Jl6zuG4fca46Q7Hy22bdpvWEddcgGiKvN3QVAyXVmJBBZbcLlFwEaPwXcmbDQwPcekl5j0nIFmoJeY9Kz7vBuwrjt0_1S7XBJwuwX--BY3_-eqr68u-NKZGwyW73nWt60VptO-eAw6Wo-9RecD2km7wb-z7V-JzbZz</recordid><startdate>20011123</startdate><enddate>20011123</enddate><creator>Haukland, H.H.</creator><creator>Ulvatne, H.</creator><creator>Sandvik, K.</creator><creator>Vorland, L.H.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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></search><sort><creationdate>20011123</creationdate><title>The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm</title><author>Haukland, H.H. ; Ulvatne, H. ; Sandvik, K. ; Vorland, L.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5523-6885811280026cb839ed3e21ebe2c860b76cf16b50d0c29d4f78a422268c61ad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Antimicrobial Cationic Peptides - metabolism</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>Antimicrobial peptide</topic><topic>BPW, Bacto peptone water</topic><topic>Cec P1, cecropin P1</topic><topic>Cecropin</topic><topic>Cell Membrane - metabolism</topic><topic>CFU, colony-forming units</topic><topic>Cytoplasm</topic><topic>Cytoplasm - metabolism</topic><topic>Cytoplasmic membrane</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - metabolism</topic><topic>Immunohistochemistry</topic><topic>Lactoferricin</topic><topic>Lactoferrin - analogs & derivatives</topic><topic>Lactoferrin - metabolism</topic><topic>Lactoferrin - pharmacology</topic><topic>Lfcin B, bovine lactoferricin</topic><topic>Mag 2, magainin 2</topic><topic>Magainin</topic><topic>Magainins</topic><topic>MBC, minimal bactericidal concentration</topic><topic>MIC, minimal inhibitory concentration</topic><topic>Microbial Sensitivity Tests</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Staphylococcus aureus - metabolism</topic><topic>TEM, transmission electron microscopy</topic><topic>Xenopus Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Haukland, H.H.</creatorcontrib><creatorcontrib>Ulvatne, H.</creatorcontrib><creatorcontrib>Sandvik, K.</creatorcontrib><creatorcontrib>Vorland, L.H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Haukland, H.H.</au><au>Ulvatne, H.</au><au>Sandvik, K.</au><au>Vorland, L.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-11-23</date><risdate>2001</risdate><volume>508</volume><issue>3</issue><spage>389</spage><epage>393</epage><pages>389-393</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The localization of immunolabelled antimicrobial peptides was studied using transmission electron microscopy.
Staphylococcus aureus and
Escherichia coli were exposed to lactoferricin B (17–41), lactoferricin B (17–31) and
D-lactoferricin B (17–31).
E. coli was also exposed to cecropin P1 and magainin 2. The lactoferricins were found in the cytoplasm of both bacteria. In
S. aureus the amount of cytoplasmic lactoferricin B (17–41) was time- and concentration-dependent, reaching a maximum within 30 min. Cecropin P1 was confined to the cell wall, while magainin 2 was found in the cytoplasm of
E. coli. The finding of intracellularly localized magainin is not reported previously.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>11728458</pmid><doi>10.1016/S0014-5793(01)03100-3</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Antimicrobial Cationic Peptides - metabolism Antimicrobial Cationic Peptides - pharmacology Antimicrobial peptide BPW, Bacto peptone water Cec P1, cecropin P1 Cecropin Cell Membrane - metabolism CFU, colony-forming units Cytoplasm Cytoplasm - metabolism Cytoplasmic membrane Escherichia coli - drug effects Escherichia coli - metabolism Immunohistochemistry Lactoferricin Lactoferrin - analogs & derivatives Lactoferrin - metabolism Lactoferrin - pharmacology Lfcin B, bovine lactoferricin Mag 2, magainin 2 Magainin Magainins MBC, minimal bactericidal concentration MIC, minimal inhibitory concentration Microbial Sensitivity Tests Staphylococcus aureus - drug effects Staphylococcus aureus - metabolism TEM, transmission electron microscopy Xenopus Proteins |
| title | The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm |
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