The Scl1 of M41-type group A Streptococcus binds the high-density lipoprotein.

Streptococcal collagen-like protein 1 (Scl1) is a virulence factor on the surface of group A Streptococcus (GAS). We have reported previously that several Scl1 proteins derived from various M-type GAS strains, including M41, can bind to low-density lipoprotein, but the Scl1 protein derived from the M6-type GAS strain cannot. Here, we demonstrated that recombinant protein, designated C176, derived from Scl1.41 of the GAS M41-type strain also binds both plasma and purified high-density lipoprotein (HDL). Next, we determined that the intact noncollagenous region of C176 was necessary and sufficient for HDL binding. C176-HDL interaction could be eliminated by the presence of low concentrations of the nonionic detergent, Tween 20, indicating the hydrophobic nature of this interaction. We finally showed that whole GAS cells expressing native Scl1.41 protein absorbed HDL from human plasma in the absence of Tween 20, but M6-type GAS cells did not. Altogether, our results add further evidence to the importance of GAS-lipoprotein binding.