An 18 kDa scaffold protein is critical for Staphylococcus epidermidis biofilm formation.
Virulence of the nosocomial pathogen Staphylococcus epidermidis is crucially linked to formation of adherent biofilms on artificial surfaces. Biofilm assembly is significantly fostered by production of a bacteria derived extracellular matrix. However, the matrix composition, spatial organization, an...
Main Authors: | , , , , , , , , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2015-03-01
|
Series: | PLoS Pathogens |
Online Access: | http://europepmc.org/articles/PMC4370877?pdf=render |
_version_ | 1818132454619217920 |
---|---|
author | Rahel Decker Christoph Burdelski Melanie Zobiak Henning Büttner Gefion Franke Martin Christner Katharina Saß Bernd Zobiak Hanae A Henke Alexander R Horswill Markus Bischoff Stephanie Bur Torsten Hartmann Carolyn R Schaeffer Paul D Fey Holger Rohde |
author_facet | Rahel Decker Christoph Burdelski Melanie Zobiak Henning Büttner Gefion Franke Martin Christner Katharina Saß Bernd Zobiak Hanae A Henke Alexander R Horswill Markus Bischoff Stephanie Bur Torsten Hartmann Carolyn R Schaeffer Paul D Fey Holger Rohde |
author_sort | Rahel Decker |
collection | DOAJ |
description | Virulence of the nosocomial pathogen Staphylococcus epidermidis is crucially linked to formation of adherent biofilms on artificial surfaces. Biofilm assembly is significantly fostered by production of a bacteria derived extracellular matrix. However, the matrix composition, spatial organization, and relevance of specific molecular interactions for integration of bacterial cells into the multilayered biofilm community are not fully understood. Here we report on the function of novel 18 kDa Small basic protein (Sbp) that was isolated from S. epidermidis biofilm matrix preparations by an affinity chromatographic approach. Sbp accumulates within the biofilm matrix, being preferentially deposited at the biofilm-substratum interface. Analysis of Sbp-negative S. epidermidis mutants demonstrated the importance of Sbp for sustained colonization of abiotic surfaces, but also epithelial cells. In addition, Sbp promotes assembly of S. epidermidis cell aggregates and establishment of multilayered biofilms by influencing polysaccharide intercellular-adhesin (PIA) and accumulation associated protein (Aap) mediated intercellular aggregation. While inactivation of Sbp indirectly resulted in reduced PIA-synthesis and biofilm formation, Sbp serves as an essential ligand during Aap domain-B mediated biofilm accumulation. Our data support the conclusion that Sbp serves as an S. epidermidis biofilm scaffold protein that significantly contributes to key steps of surface colonization. Sbp-negative S. epidermidis mutants showed no attenuated virulence in a mouse catheter infection model. Nevertheless, the high prevalence of sbp in commensal and invasive S. epidermidis populations suggests that Sbp plays a significant role as a co-factor during both multi-factorial commensal colonization and infection of artificial surfaces. |
first_indexed | 2024-12-11T08:37:05Z |
format | Article |
id | doaj.art-ccb8804bc78a49ea9f772ba22188c9c0 |
institution | Directory Open Access Journal |
issn | 1553-7366 1553-7374 |
language | English |
last_indexed | 2024-12-11T08:37:05Z |
publishDate | 2015-03-01 |
publisher | Public Library of Science (PLoS) |
record_format | Article |
series | PLoS Pathogens |
spelling | doaj.art-ccb8804bc78a49ea9f772ba22188c9c02022-12-22T01:14:20ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742015-03-01113e100473510.1371/journal.ppat.1004735An 18 kDa scaffold protein is critical for Staphylococcus epidermidis biofilm formation.Rahel DeckerChristoph BurdelskiMelanie ZobiakHenning BüttnerGefion FrankeMartin ChristnerKatharina SaßBernd ZobiakHanae A HenkeAlexander R HorswillMarkus BischoffStephanie BurTorsten HartmannCarolyn R SchaefferPaul D FeyHolger RohdeVirulence of the nosocomial pathogen Staphylococcus epidermidis is crucially linked to formation of adherent biofilms on artificial surfaces. Biofilm assembly is significantly fostered by production of a bacteria derived extracellular matrix. However, the matrix composition, spatial organization, and relevance of specific molecular interactions for integration of bacterial cells into the multilayered biofilm community are not fully understood. Here we report on the function of novel 18 kDa Small basic protein (Sbp) that was isolated from S. epidermidis biofilm matrix preparations by an affinity chromatographic approach. Sbp accumulates within the biofilm matrix, being preferentially deposited at the biofilm-substratum interface. Analysis of Sbp-negative S. epidermidis mutants demonstrated the importance of Sbp for sustained colonization of abiotic surfaces, but also epithelial cells. In addition, Sbp promotes assembly of S. epidermidis cell aggregates and establishment of multilayered biofilms by influencing polysaccharide intercellular-adhesin (PIA) and accumulation associated protein (Aap) mediated intercellular aggregation. While inactivation of Sbp indirectly resulted in reduced PIA-synthesis and biofilm formation, Sbp serves as an essential ligand during Aap domain-B mediated biofilm accumulation. Our data support the conclusion that Sbp serves as an S. epidermidis biofilm scaffold protein that significantly contributes to key steps of surface colonization. Sbp-negative S. epidermidis mutants showed no attenuated virulence in a mouse catheter infection model. Nevertheless, the high prevalence of sbp in commensal and invasive S. epidermidis populations suggests that Sbp plays a significant role as a co-factor during both multi-factorial commensal colonization and infection of artificial surfaces.http://europepmc.org/articles/PMC4370877?pdf=render |
spellingShingle | Rahel Decker Christoph Burdelski Melanie Zobiak Henning Büttner Gefion Franke Martin Christner Katharina Saß Bernd Zobiak Hanae A Henke Alexander R Horswill Markus Bischoff Stephanie Bur Torsten Hartmann Carolyn R Schaeffer Paul D Fey Holger Rohde An 18 kDa scaffold protein is critical for Staphylococcus epidermidis biofilm formation. PLoS Pathogens |
title | An 18 kDa scaffold protein is critical for Staphylococcus epidermidis biofilm formation. |
title_full | An 18 kDa scaffold protein is critical for Staphylococcus epidermidis biofilm formation. |
title_fullStr | An 18 kDa scaffold protein is critical for Staphylococcus epidermidis biofilm formation. |
title_full_unstemmed | An 18 kDa scaffold protein is critical for Staphylococcus epidermidis biofilm formation. |
title_short | An 18 kDa scaffold protein is critical for Staphylococcus epidermidis biofilm formation. |
title_sort | 18 kda scaffold protein is critical for staphylococcus epidermidis biofilm formation |
url | http://europepmc.org/articles/PMC4370877?pdf=render |
work_keys_str_mv | AT raheldecker an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT christophburdelski an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT melaniezobiak an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT henningbuttner an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT gefionfranke an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT martinchristner an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT katharinasaß an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT berndzobiak an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT hanaeahenke an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT alexanderrhorswill an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT markusbischoff an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT stephaniebur an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT torstenhartmann an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT carolynrschaeffer an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT pauldfey an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT holgerrohde an18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT raheldecker 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT christophburdelski 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT melaniezobiak 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT henningbuttner 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT gefionfranke 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT martinchristner 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT katharinasaß 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT berndzobiak 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT hanaeahenke 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT alexanderrhorswill 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT markusbischoff 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT stephaniebur 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT torstenhartmann 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT carolynrschaeffer 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT pauldfey 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation AT holgerrohde 18kdascaffoldproteiniscriticalforstaphylococcusepidermidisbiofilmformation |