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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Characterisation of SEQ0694 (PrsA/PrtM) of Streptococcus equi as a functional peptidyl-prolyl isomerase affecting

Felicia Ikolo1, Meng Zhang2, Dean J Harrington3

  • 1Department of Applied Sciences, Faculty of Health & Life Sciences, University of Northumbria at Newcastle, Newcastle upon Tyne, NE1 8ST, UK. iain.sutcliffe@northumbria.ac.uk and Department of Biochemistry, School of Medicine, St. George's University, True Blue, St. George's, Grenada.

Molecular Biosystems
|October 15, 2015
PubMed

Insights

Streptococcus equi

Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Protein Folding

Background:

  • Peptidyl-prolyl isomerase (PPIase) lipoproteins are crucial for virulence in Gram-positive pathogens.
  • These proteins likely aid in folding cell envelope and secreted virulence factors.

Purpose of the Study:

  • To investigate the role of Streptococcus equi PPIase SEQ0694 in virulence.
  • To determine if SEQ0694 affects the production of secreted proteins.

Main Methods:

  • Proteomic analysis of Streptococcus equi.
  • Biochemical characterization of recombinant SEQ0694 and its parvulin domain.

Main Results:

  • SEQ0694 was shown to alter the production of multiple secreted proteins, including virulence factors FNE and IdeE2.
  • Recombinant SEQ0694 and its parvulin domain were confirmed as functional PPIases.
  • Unusual sequence features in SEQ0694 do not impede its enzymatic activity.

Conclusions:

  • Lipoprotein PPIases, like SEQ0694, contribute to Streptococcus virulence.
  • Understanding these mechanisms can inform strategies against streptococcal pathogens.

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