Research

Staphylococcus aureus Proteins Sbi and Efb Recruit Human Plasmin to Degrade Complement C3 and C3b


Reference:

Koch, T. K., Reuter, M., Barthel, D., Böhm, S., Van Den Elsen, J., Kraiczy, P., Zipfel, P. F. and Skerka, C., 2012. Staphylococcus aureus Proteins Sbi and Efb Recruit Human Plasmin to Degrade Complement C3 and C3b. PLoS ONE, 7 (10), e47638.

Related documents:

This repository does not currently have the full-text of this item.
You may be able to access a copy if URLs are provided below. (Contact Author)

Official URL:

http://dx.doi.org/10.1371/journal.pone.0047638

Related URLs:

Abstract

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.

Details

Item Type Articles
CreatorsKoch, T. K., Reuter, M., Barthel, D., Böhm, S., Van Den Elsen, J., Kraiczy, P., Zipfel, P. F. and Skerka, C.
DOI10.1371/journal.pone.0047638
Related URLs
URLURL Type
http://www.scopus.com/inward/record.url?scp=84867415024&partnerID=8YFLogxKUNSPECIFIED
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code32768

Export

Actions (login required)

View Item