Staphylococcus aureus proteins Sbi and Efb recruit human plasmin to degrade complement C3 and C3b

Upon host infection, the human pathogenic microbe Staphylococcus aureus (S. aureus) immediately faces innate immune reactions such as the activated complement system. Here, a novel innate immune evasion strategy of S. aureus is described. The staphylococcal proteins surface immunoglobulin-binding pr...

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Bibliographic Details
Published in:	PloS one Vol. 7; no. 10; p. e47638
Main Authors:	Koch, Tina K, Reuter, Michael, Barthel, Diana, Böhm, Sascha, van den Elsen, Jean, Kraiczy, Peter, Zipfel, Peter F, Skerka, Christine
Format:	Journal Article
Language:	English
Published:	United States Public Library of Science 11-10-2012 Public Library of Science (PLoS)
Subjects:	Bacteria Bacterial proteins Bacterial Proteins - metabolism Biodegradation Biology Blotting, Western Borrelia burgdorferi Candida albicans Carrier Proteins - metabolism Cloning, Molecular Complement Complement activation Complement C3 - metabolism Complement C3b - metabolism Complement component C3 Complement component C3b Complement Inactivator Proteins - metabolism Complement system Degradation Development and progression DNA Primers - genetics Enzyme-Linked Immunosorbent Assay Extracellular matrix Fibrinogen Fibrinogen-binding protein Fibrinolysin - metabolism Genetic aspects Health aspects Humans Immunity, Innate - immunology Immunology Infectious diseases Medicine Microorganisms Natural products Pathogens Physiological aspects Plasmin Plasminogen - metabolism Proteins Proteolysis Staphylococcus aureus Staphylococcus aureus - immunology Staphylococcus aureus infections Staphylococcus infections Staphylokinase Surface Plasmon Resonance U-Plasminogen activator Urokinase Germany
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Summary:	Upon host infection, the human pathogenic microbe Staphylococcus aureus (S. aureus) immediately faces innate immune reactions such as the activated complement system. Here, a novel innate immune evasion strategy of S. aureus is described. The staphylococcal proteins surface immunoglobulin-binding protein (Sbi) and extracellular fibrinogen-binding protein (Efb) bind C3/C3b simultaneously with plasminogen. Bound plasminogen is converted by bacterial activator staphylokinase or by host-specific urokinase-type plasminogen activator to plasmin, which in turn leads to degradation of complement C3 and C3b. Efb and to a lesser extend Sbi enhance plasmin cleavage of C3/C3b, an effect which is explained by a conformational change in C3/C3b induced by Sbi and Efb. Furthermore, bound plasmin also degrades C3a, which exerts anaphylatoxic and antimicrobial activities. Thus, S. aureus Sbi and Efb comprise platforms to recruit plasmin(ogen) together with C3 and its activation product C3b for efficient degradation of these complement components in the local microbial environment and to protect S. aureus from host innate immune reactions.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Conceived and designed the experiments: CS TKK. Performed the experiments: TKK MR DB SB. Analyzed the data: TKK MR DB SB JvdE PFZ PK CS. Contributed reagents/materials/analysis tools: DB PK SB. Wrote the paper: TKK PFZ CS. Competing Interests: The authors have declared that no competing interests exist.
ISSN:	1932-6203 1932-6203
DOI:	10.1371/journal.pone.0047638