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- W4387250906 abstract "Abstract Generally, Staphylococcus aureus biofilms are composed of proteins, extracellular DNA (eDNA), and polysaccharide intercellular adhesin (PIA). Our knowledge of biofilm development is largely derived from in vitro systems. The molecular mechanisms underlying in vivo biofilm formation remain unclear. We analyzed murine catheter-associated biofilms through a proteomic approach and demonstrated the potential development process of the in vivo biofilm matrix. The biofilm-forming capacity of different S. aureus strains was evaluated through the classical static biofilm assay in vitro or subcutaneous implantation of a catheter infection model in mice. The protein composition of the in vivo biofilm matrix was analyzed through a proteomic approach. An albumin pull-down assay was employed to identify cell wall proteins interacting with albumin, followed by characterization using a bacterial adhesion assay. The expression levels of biofilm-associated genes were determined using qRT-PCR. The S. aureus strains used in this study produced exopolysaccharide-rich biofilms in vitro but proteinaceous biofilm matrices in vivo . Proteomic analysis showed that albumin was one of the most abundant proteins in the in vivo biofilms and was specifically incorporated into the biofilm matrix. Staphylococcal fibronectin-binding proteins were characterized as binding with albumin to form biofilms that were stabilized with eDNA. The production of PIA was suppressed in the presence of albumin. In vitro biofilm nonproducers may utilize host factors to form biofilms in vivo . We demonstrated that S. aureus used different strategies to develop biofilms in vitro and in vivo . Our study provides insight into the strategies used in eradicating biofilms in hosts." @default.
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- W4387250906 date "2023-10-02" @default.
- W4387250906 modified "2023-10-03" @default.
- W4387250906 title "The in vivo biofilm formation of Staphylococcus aureus in a mouse model: albumin is the major biofilm matrix" @default.
- W4387250906 doi "https://doi.org/10.21203/rs.3.rs-3368672/v1" @default.
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