Relatedness between the two-component lantibiotics lacticin 3147 and staphylococcin C55 based on structure, genetics and biological activity

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dc.contributor.author O'Connor, Eileen B.
dc.contributor.author Cotter, Paul D.
dc.contributor.author O'Connor, Paula M.
dc.contributor.author O'Sullivan, Orla
dc.contributor.author Tagg, John R.
dc.contributor.author Ross, R. Paul
dc.contributor.author Hill, Colin
dc.date.accessioned 2012-12-12T09:50:52Z
dc.date.available 2012-12-12T09:50:52Z
dc.date.copyright 2007
dc.date.issued 2007-04-02
dc.identifier.citation O'Connor, E. and Cotter, P. and O'Connor, P. and O'Sullivan, O. and Tagg, J. and Ross, R.P. and Hill, C. (2007) 'Relatedness between the two-component lantibiotics lacticin 3147 and staphylococcin C55 based on structure, genetics and biological activity'. BMC microbiology, 7 (24). doi: 10.1186/1471-2180-7-24 en
dc.identifier.volume 7 en
dc.identifier.startpage 24 en
dc.identifier.issn 1471-2180
dc.identifier.uri http://hdl.handle.net/10468/841
dc.identifier.doi 10.1186/1471-2180-7-24
dc.description.abstract Background: Two component lantibiotics, such as the plasmid-encoded lacticin 3147 produced by Lactococcus lactis DPC3147 and staphylococcin C55 produced by Staphylococcus aureus C55, represent an emerging subgroup of bacteriocins. These two bacteriocins are particularly closely related, exhibiting 86% (LtnA1 and C55α) and 55% (LtnA2 and C55β) identity in their component peptides. The aim of this study was to investigate, for the first time for any two component bacteriocins, the significance of the relatedness between these two systems. Results: So close is this relatedness that the hybrid peptide pairs LtnA1:C55β and C55α:LtnA2 were found to have activities in the single nanomolar range, comparing well with the native pairings. To determine whether this flexibility extended to the associated post-translational modification/processing machinery, the staphylococcin C55 structural genes were directly substituted for their lacticin 3147 counterparts in the ltn operon on the large conjugative lactococcal plasmid pMRC01. It was established that the lacticin LtnA1 post-translational and processing machinery could produce functionally active C55α, but not C55β. In order to investigate in closer detail the significance of the differences between LtnA1 and C55α, three residues in LtnA1 were replaced with the equivalent residues in C55α. Surprisingly, one such mutant LtnA1-Leu21Ala was not produced. This may be significant given the positioning of this residue in a putative lipid II binding loop. Conclusion: It is apparent, despite sharing striking similarities in terms of structure and activity, that these two complex bacteriocins display some highly dedicated features particular to either system. en
dc.description.sponsorship Science Foundation Ireland (SFI-CSET);Irish Government (National Development Plan 2000–2006); Teagasc (Walsh Fellowship) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher BioMed Central en
dc.relation.uri http://www.biomedcentral.com/1471-2180/7/24
dc.rights © 2007 O'Connor et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. en
dc.rights.uri http://creativecommons.org/licenses/by/2.0/ en
dc.subject Lacticin en
dc.subject Staphylococcin en
dc.subject Relatedness en
dc.subject Lantibiotics en
dc.subject Bacteriocins en
dc.subject Processing machinery en
dc.title Relatedness between the two-component lantibiotics lacticin 3147 and staphylococcin C55 based on structure, genetics and biological activity en
dc.type Article (peer-reviewed) en
dc.internal.authorurl http://publish.ucc.ie/researchprofiles/D010/chill en
dc.internal.authorcontactother Colin Hill, Department of Microbiology, University College Cork, Ireland. Email: c.hill@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.internal.rssid 121848194
dc.contributor.funder Science Foundation Ireland en
dc.contributor.funder Irish Government en
dc.contributor.funder Teagasc en
dc.description.status Peer reviewed en
dc.identifier.journaltitle BMC Microbiology en
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dc.internal.IRISemailaddress c.hill@ucc.ie en


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© 2007 O'Connor et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Except where otherwise noted, this item's license is described as © 2007 O'Connor et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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