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dc.date.accessioned2018-09-25T15:11:09Z
dc.date.available2018-09-25T15:11:09Z
dc.date.created2017-05-05T09:34:08Z
dc.date.issued2017
dc.identifier.citationOvchinnikov, Kirill Kristiansen, Per Eugen Straume, Daniel Jensen, Marianne Slang Aleksandrzak-Piekarczyk, Tamara Nes, Ingolf Diep, Dzung Bao . The leaderless bacteriocin enterocin K1 is highly potent against Enterococcus faecium: A study on structure, target spectrum and receptor. Frontiers in Microbiology. 2017, 8, 1-12
dc.identifier.urihttp://hdl.handle.net/10852/64959
dc.description.abstractEnterocin K1 (EntK1), enterocin EJ97 (EntEJ97), and LsbB are three sequence related leaderless bacteriocins. Yet LsbB kills only lactococci while EntK1 and EntEJ97 target wider spectra with EntK1 being particularly active against Enterococcus faecium, including nosocomial multidrug resistant isolates. NMR study of EntK1 showed that it had a structure very similar to LsbB – both having an amphiphilic N-terminal α-helix and an unstructured C-terminus. The α-helix in EntK1 is, however, about 3–4 residues longer than that of LsbB. Enterococcal mutants highly resistant to EntEJ97 and EntK1 were found to have mutations within rseP, a gene encoding a stress response membrane-bound Zn-dependent protease. Heterologous expression of the enterococcal rseP rendered resistant cells of Streptococcus pneumoniae sensitive to EntK1 and EntEJ97, suggesting that RseP likely serves as the receptor for EntK1 and EntEJ97. It was also shown that the conserved proteolytic active site in E. faecalis RseP is partly required for EntK1 and EntEJ97 activity, since alanine substitutions of its conserved residues (HExxH) reduced the sensitivity of the clones to the bacteriocins. RseP is known to be involved in bacterial stress response. As expected, the growth of resistant mutants with mutations within rseP was severely affected when they were exposed to higher (stressing) growth temperatures, e.g., at 45∘C, at which wild type cells still grew well. These findings allow us to design a hurdle strategy with a combination of the bacteriocin(s) and higher temperature that effectively kills bacteriocin sensitive bacteria and prevents the development of resistant cells.en_US
dc.languageEN
dc.publisherFrontiers Research Foundation
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleThe leaderless bacteriocin enterocin K1 is highly potent against Enterococcus faecium: A study on structure, target spectrum and receptoren_US
dc.title.alternativeENEngelskEnglishThe leaderless bacteriocin enterocin K1 is highly potent against Enterococcus faecium: A study on structure, target spectrum and receptor
dc.typeJournal articleen_US
dc.creator.authorOvchinnikov, Kirill
dc.creator.authorKristiansen, Per Eugen
dc.creator.authorStraume, Daniel
dc.creator.authorJensen, Marianne Slang
dc.creator.authorAleksandrzak-Piekarczyk, Tamara
dc.creator.authorNes, Ingolf
dc.creator.authorDiep, Dzung Bao
cristin.unitcode185,15,29,40
cristin.unitnameSeksjon for biokjemi og molekylærbiologi
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1
dc.identifier.cristin1468299
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Frontiers in Microbiology&rft.volume=8&rft.spage=1&rft.date=2017
dc.identifier.jtitleFrontiers in Microbiology
dc.identifier.volume8
dc.identifier.startpage1
dc.identifier.endpage12
dc.identifier.doihttp://dx.doi.org/10.3389/fmicb.2017.00774
dc.identifier.urnURN:NBN:no-67489
dc.type.documentTidsskriftartikkelen_US
dc.type.peerreviewedPeer reviewed
dc.source.issn1664-302X
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/64959/2/fmicb-08-00774.pdf
dc.type.versionPublishedVersion
cristin.articleid774
dc.relation.projectNFR/254784


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