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

Ikolo, Felicia, Zhang, Meng, Harrington, Dean, Robinson, Carl, Waller, Andrew, Sutcliffe, Iain and Black, Gary (2015) Characterisation of SEQ0694 (PrsA/PrtM) of Streptococcus equi as a functional peptidyl-prolyl isomerase affecting multiple secreted protein substrates. Molecular BioSystems, 11. pp. 3279-3286. ISSN 1742-206X

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Official URL: http://dx.doi.org/10.1039/C5MB00543D

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.

Item Type: Article
Subjects: C700 Molecular Biology, Biophysics and Biochemistry
Department: Faculties > Health and Life Sciences > School of Life Sciences > Applied Sciences
Depositing User: Becky Skoyles
Date Deposited: 03 Nov 2015 11:08
Last Modified: 15 May 2017 10:26
URI: http://nrl.northumbria.ac.uk/id/eprint/24277

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