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Protein SIC, a novel extracellular protein of Streptococcus pyogenes interfering with complement function

P Akesson¹, A G Sjöholm, L Björck

¹Department of Cell and Molecular Biology, Lund University, Sweden.

The Journal of Biological Chemistry

|January 12, 1996

Summary

A novel Streptococcus pyogenes protein, SIC, inhibits complement-mediated lysis by binding clusterin and HRG. This protein is found in M1 and M57 serotypes, potentially explaining the rise in severe infections.

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Area of Science:

Microbiology
Immunology
Molecular Biology

Background:

Streptococcus pyogenes virulence is regulated by the mga regulon.
M1 serotype strains are increasingly associated with severe infections.

Purpose of the Study:

To identify and characterize novel virulence factors in Streptococcus pyogenes.
To investigate the role of a newly discovered protein in complement evasion.

Main Methods:

Gene cloning and sequencing of a novel S. pyogenes protein.
Protein purification and characterization.
Interaction studies with human plasma proteins (clusterin, HRG) and complement components.

Main Results:

A novel protein, designated SIC (streptococcal inhibitor of complement-mediated lysis), was identified.

Related Experiment Videos

SIC binds to human clusterin and histidine-rich glycoprotein (HRG).

SIC inhibits complement-mediated lysis and is incorporated into the C5b-C9 complex.

SIC is present in M1 and M57 S. pyogenes serotypes.

Conclusions:

Protein SIC is a novel virulence factor that inhibits complement-mediated lysis.
SIC's presence in M1 strains may contribute to the increased severity of infections.
Further research into SIC could lead to new therapeutic strategies against S. pyogenes.