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dc.contributor.authorIkolo, F.*
dc.contributor.authorZhang, M.*
dc.contributor.authorHarrington, Dean J.*
dc.contributor.authorRobinson, C.*
dc.contributor.authorWaller, A.S.*
dc.contributor.authorSutcliffe, I.C.*
dc.contributor.authorBlack, G.W.*
dc.date.accessioned2016-11-14T15:47:32Z
dc.date.available2016-11-14T15:47:32Z
dc.date.issued2015
dc.identifier.citationIkolo F, Zhang M, Harrison DJ et al (2015) Characterisation of SEQ0694 (PrsA/PrtM) of Streptococcus equi as a functional peptidyl-prolyl isomerase affecting multiple secreted protein substrates. Molecular BioSystems. 11(12): 3279-3286.
dc.identifier.urihttp://hdl.handle.net/10454/10324
dc.descriptionYes
dc.description.abstractPeptidyl-prolyl isomerase (PPIase) lipoproteins have been shown to influence the virulence of a number of Gram-positive bacterial human and animal pathogens, most likely through facilitating the folding of cell envelope and secreted virulence factors. Here, we used a proteomic approach to demonstrate that the Streptococcus equi PPIase SEQ0694 alters the production of multiple secreted proteins, including at least two putative virulence factors (FNE and IdeE2). We demonstrate also that, despite some unusual sequence features, recombinant SEQ0694 and its central parvulin domain are functional PPIases. These data add to our knowledge of the mechanisms by which lipoprotein PPIases contribute to the virulence of streptococcal pathogens.
dc.language.isoen
dc.rights© 2015 Royal Society of Chemistry. This is an Open Access article published under the Creative Commons CC-BY license (http://creativecommons.org/licenses/by/3.0/)
dc.subjectStreptococcus equi
dc.subjectSEQ0694
dc.subjectVirulence
dc.subjectHuman pathogens
dc.subjectAnimal pathogens
dc.subjectLipoprotein PPlases
dc.titleCharacterisation of SEQ0694 (PrsA/PrtM) of Streptococcus equi as a functional peptidyl-prolyl isomerase affecting multiple secreted protein substrates
dc.status.refereedYes
dc.date.Accepted08/10/2015
dc.date.application08/10/2015
dc.typeArticle
dc.type.versionPublished version
dc.identifier.doihttps://doi.org/10.1039/c5mb00543d
dc.rights.licenseCC-BY
refterms.dateFOA2018-07-27T01:42:57Z
dc.openaccess.statusopenAccess


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