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    Characterisation of SEQ0694 (PrsA/PrtM) of Streptococcus equi as a functional peptidyl-prolyl isomerase affecting multiple secreted protein substrates

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    Publication date
    2015
    Author
    Ikolo, F.
    Zhang, M.
    Harrington, Dean J.
    Robinson, C.
    Waller, A.S.
    Sutcliffe, I.C.
    Black, G.W.
    Keyword
    Streptococcus equi; SEQ0694; Virulence; Human pathogens; Animal pathogens; Lipoprotein PPlases
    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/)
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    Peptidyl-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.
    URI
    http://hdl.handle.net/10454/10324
    Version
    Published version
    Citation
    Ikolo 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.
    Link to publisher’s version
    http://dx.doi.org/10.1039/c5mb00543d
    Type
    Article
    Collections
    Life Sciences Publications

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