The fibronectin-binding capacity and host cell adherence of Streptococcus pyogenes strains are discordant with each other.

Surface exposed fibronectin-binding proteins (FBPs) play an important role in the adherence of Streptococcus pyogenes (group A streptococcus, GAS) to host cells. This pathogen expresses numerous FBPs, of which SfbI, SfbII and PrtF2 are major surface exposed FBPs. However, GAS strains differ in the genetic potential to express these proteins.

Inhibition of Streptococcus pyogenes adherence to HaCaT cells by a peptide corresponding to the streptococcal fibronectin-binding protein, SfbI, is strain dependent.

Streptococcus pyogenes (group A streptococcus, GAS) is a human-specific pathogen, which employs a large number of adhesins for colonization. Fibronectin-binding proteins (FBPs) play a major role in GAS adhesion to host cells. SfbI, a major streptococcal FBP, has been well studied.

Strains of Streptococcus pyogenes from severe invasive infections bind HEp2 and HaCaT cells more avidly than strains from uncomplicated infections.

Epidemiologically unrelated Streptococcus pyogenes strains isolated from blood, throat, and skin were assayed for adherence to HEp2 and HaCaT cells. Invasive isolates showed significantly higher avidity for these cell lines than isolates from skin and throat. In general, S.