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SufA - a bacterial enzyme that cleaves fibrinogen and blocks fibrin network formation
Christofer Karlsson1, Matthias Mörgelin1, Mattias Collin1
1Division of Infection Medicine, Department of Clinical Sciences, Lund University, BMC B14, 221 84 Lund, Sweden.
Abstract:
Finegoldia magna is a member of the normal human bacterial flora on the skin and other non-sterile body surfaces, but this anaerobic coccus is also an important opportunistic pathogen. SufA was the first F. magna proteinase to be isolated and characterized. Many bacterial pathogens interfere with different steps of blood coagulation, and here we describe how purified SufA efficiently and specifically cleaves fibrinogen in human plasma. SufA is both secreted by F. magna and associated with the bacterial surface. Successful gene targeting has previously not been performed in anaerobic cocci, but in order to study the role of the SufA that is present at the bacterial surface, we constructed an F. magna mutant that expresses a truncated SufA lacking proteolytic activity. In contrast to wild-type bacteria that delayed the coagulation of human plasma, mutant bacteria had no such effect. Wild-type and mutant bacteria adhered to keratinocytes equally well, but in a plasma environment only wild-type bacteria blocked the formation of fibrin networks surrounding adherent bacteria. The effective cleavage of fibrinogen by SufA suggests that the interference with fibrin network formation represents an adaptive mechanism of F. magna with potential implications also for pathogenicity.
Insights
Finegoldia magna
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Biochemistry
Background:
- Finegoldia magna is a commensal bacterium and opportunistic pathogen.
- SufA is a proteinase secreted by F. magna.
- Bacterial pathogens can interfere with blood coagulation.
Purpose of the Study:
- To investigate the role of F. magna SufA in fibrinogen cleavage and blood coagulation.
- To characterize the function of surface-associated SufA in F. magna.
- To explore the implications of SufA activity in bacterial adaptation and pathogenicity.
Main Methods:
- Purified SufA was used to cleave human plasma fibrinogen.
- Gene targeting was employed to create an F. magna mutant lacking active SufA.
- Coagulation assays and bacterial adhesion studies were performed.
Main Results:
- Purified SufA efficiently cleaved fibrinogen in human plasma.
- F. magna mutant bacteria did not delay plasma coagulation.
- Wild-type F. magna, but not the mutant, blocked fibrin network formation around adherent bacteria in plasma.
Conclusions:
- F. magna SufA cleaves fibrinogen, interfering with fibrin network formation.
- Surface-associated SufA plays a role in F. magna's interaction with plasma.
- This mechanism may represent an adaptive strategy for F. magna with implications for pathogenicity.
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