Details

Autor(en) / Beteiligte

• Haupt, Katrin
• Reuter, Michael
• Elsen, Jean vanden
• Burman, Julia
• Hälbich, Steffi
• Richter, Julia
• Skerka, Christine
• Zipfel, Peter F

Titel

The Staphylococcus aureus Protein Sbi Acts as a Complement Inhibitor and Forms a Tripartite Complex with Host Complement Factor H and C3b: e1000250

Ist Teil von

• PLoS pathogens, 2008-12, Vol.4 (12)

Ort / Verlag

San Francisco: Public Library of Science

Erscheinungsjahr

2008

Quelle

EZB*

Beschreibungen/Notizen

• The Gram-positive bacterium Staphylococcus aureus, similar to other pathogens, binds human complement regulators Factor H and Factor H related protein 1 (FHR-1) from human serum. Here we identify the secreted protein Sbi (Staphylococcus aureus binder of IgG) as a ligand that interacts with Factor H by a--to our knowledge--new type of interaction. Factor H binds to Sbi in combination with C3b or C3d, and forms tripartite Sbi:C3:Factor H complexes. Apparently, the type of C3 influences the stability of the complex; surface plasmon resonance studies revealed a higher stability of C3d complexed to Sbi, as compared to C3b or C3. As part of this tripartite complex, Factor H is functionally active and displays complement regulatory activity. Sbi, by recruiting Factor H and C3b, acts as a potent complement inhibitor, and inhibits alternative pathway-mediated lyses of rabbit erythrocytes by human serum and sera of other species. Thus, Sbi is a multifunctional bacterial protein, which binds host complement components Factor H and C3 as well as IgG and β2-glycoprotein I and interferes with innate immune recognition.