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Flotillin scaffold activity contributes to type VII secretion system assembly in Staphylococcus aureus

Please always quote using this URN: urn:nbn:de:bvb:20-opus-170035
  • Scaffold proteins are ubiquitous chaperones that promote efficient interactions between partners of multi-enzymatic protein complexes; although they are well studied in eukaryotes, their role in prokaryotic systems is poorly understood. Bacterial membranes have functional membrane microdomains (FMM), a structure homologous to eukaryotic lipid rafts. Similar to their eukaryotic counterparts, bacterial FMM harbor a scaffold protein termed flotillin that is thought to promote interactions between proteins spatially confined to the FMM. Here weScaffold proteins are ubiquitous chaperones that promote efficient interactions between partners of multi-enzymatic protein complexes; although they are well studied in eukaryotes, their role in prokaryotic systems is poorly understood. Bacterial membranes have functional membrane microdomains (FMM), a structure homologous to eukaryotic lipid rafts. Similar to their eukaryotic counterparts, bacterial FMM harbor a scaffold protein termed flotillin that is thought to promote interactions between proteins spatially confined to the FMM. Here we used biochemical approaches to define the scaffold activity of the flotillin homolog FloA of the human pathogen Staphylococcus aureus, using assembly of interacting protein partners of the type VII secretion system (T7SS) as a case study. Staphylococcus aureus cells that lacked FloA showed reduced T7SS function, and thus reduced secretion of T7SS-related effectors, probably due to the supporting scaffold activity of flotillin. We found that the presence of flotillin mediates intermolecular interactions of T7SS proteins. We tested several small molecules that interfere with flotillin scaffold activity, which perturbed T7SS activity in vitro and in vivo. Our results suggest that flotillin assists in the assembly of S. aureus membrane components that participate in infection and influences the infective potential of this pathogen.show moreshow less

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Metadaten
Author: Benjamin Mielich-Süss, Rabea M. Wagner, Nicole Mietrach, Tobias Hertlein, Gabriella Marincola, Knut Ohlsen, Sebastian Geibel, Daniel Lopez
URN:urn:nbn:de:bvb:20-opus-170035
Document Type:Journal article
Faculties:Medizinische Fakultät / Institut für Molekulare Infektionsbiologie
Fakultät für Biologie / Rudolf-Virchow-Zentrum
Language:English
Parent Title (English):PLoS Pathogens
Year of Completion:2017
Volume:13
Issue:11
Pagenumber:e1006728
Source:PLoS Pathogens 13(11):e1006728 (2017). DOI: 10.1371/journal.ppat.1006728
DOI:https://doi.org/10.1371/journal.ppat.1006728
Pubmed Id:http://www.ncbi.nlm.nih.gov/pubmed?term=29166667
Dewey Decimal Classification:6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit
Tag:Staphylococcus aureus; flotillin; scaffold protein; type VII secretion system
Release Date:2019/09/18
EU-Project number / Contract (GA) number:ERC335568
OpenAIRE:OpenAIRE
Licence (German):License LogoCC BY: Creative-Commons-Lizenz: Namensnennung 4.0 International