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Heterogeneity in ess transcriptional organization and variable contribution of the Ess/Type VII protein secretion system to virulence across closely related Staphylocccus aureus strains

Title: Heterogeneity in ess transcriptional organization and variable contribution of the Ess/Type VII protein secretion system to virulence across closely related Staphylocccus aureus strains
Authors: Kneuper H; Cao ZP; Twomey KB; Zoltner M; Jager F; Cargill JS; Chalmers J; van der Kooi-Pol MM; van Dijl JM; Ryan RP; Hunter WN; Palmer T
Source: Molecular Microbiology, September 2014
Publisher Information: Wiley-Blackwell Publishing Ltd.
Publication Year: 2014
Collection: Newcastle University Library ePrints Service
Description: Summary: The Type VII protein secretion system, found in Gram-positive bacteria, secretes small proteins, containing a conserved W-x-G amino acid sequence motif, to the growth medium. Staphylococcus aureus has a conserved Type VII secretion system, termed Ess, which is dispensable for laboratory growth but required for virulence. In this study we show that there are unexpected differences in the organization of the ess gene cluster between closely related strains of S. aureus. We further show that in laboratory growth medium different strains of S. aureus secrete the EsxA and EsxC substrate proteins at different growth points, and that the Ess system in strain Newman is inactive under these conditions. Systematic deletion analysis in S. aureusRN6390 is consistent with the EsaA, EsaB, EssA, EssB, EssC and EsxA proteins comprising core components of the secretion machinery in this strain. Finally we demonstrate that the Ess secretion machinery of two S. aureus strains, RN6390 and COL, is important for nasal colonization and virulence in the murine lung pneumonia model. Surprisingly, however, the secretion system plays no role in the virulence of strain SA113 under the same conditions. © 2014 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.
Document Type: article in journal/newspaper
File Description: application/pdf
Language: unknown
Relation: https://eprints.ncl.ac.uk/255091; https://eprints.ncl.ac.uk/fulltext.aspx?url=255091/4688D2E8-2B15-4CD0-B924-FA7D75981886.pdf&pub_id=255091
Availability: https://eprints.ncl.ac.uk/255091
Rights: https://creativecommons.org/licenses/by/4.0/
Accession Number: edsbas.811AF8
Database: BASE