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Merck
  • Attenuating Staphylococcus aureus Virulence by Targeting Flotillin Protein Scaffold Activity.

Attenuating Staphylococcus aureus Virulence by Targeting Flotillin Protein Scaffold Activity.

Cell chemical biology (2017-07-04)
Gudrun Koch, Charlotte Wermser, Ivan C Acosta, Lara Kricks, Stephanie T Stengel, Ana Yepes, Daniel Lopez
摘要

Scaffold proteins are ubiquitous chaperones that bind proteins and facilitate physical interaction of multi-enzyme complexes. Here we used a biochemical approach to dissect the scaffold activity of the flotillin-homolog protein FloA of the multi-drug-resistant human pathogen Staphylococcus aureus. We show that FloA promotes oligomerization of membrane protein complexes, such as the membrane-associated RNase Rny, which forms part of the RNA-degradation machinery called the degradosome. Cells lacking FloA had reduced Rny function and a consequent increase in the targeted sRNA transcripts that negatively regulate S. aureus toxin expression. Small molecules that altered FloA oligomerization also reduced Rny function and decreased the virulence potential of S. aureus in vitro, as well as in vivo, using invertebrate and murine infection models. Our results suggest that flotillin assists in the assembly of protein complexes involved in S. aureus virulence, and could thus be an attractive target for the development of new antimicrobial therapies.

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Millipore
抗-FLAG® 兔抗, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
S-亚硝基-N-乙酰基-DL-青霉胺, ≥97%, powder
Sigma-Aldrich
扎格雷酸 A 三钠盐, ≥95% (HPLC), microbial