Epidemiologically and clinically relevant Group B Streptococcus isolates do not bind collagen but display enhanced binding to human fibrinogen.

International audienceGroup B Streptococcus (GBS) is the leading cause of neonatal septicemia and meningitis. Pili appendages were shown to play a critical role in bacterial adhesion and colonization of human tissues. Recently it was claimed that binding of the pilus-associated adhesin PilA to collagen is a critical, initial step in promoting interactions with the α2β1 integrin expressed on brain endothelial cells. Here we show that strain NCTC10/84 used in this study is not representative for GBS isolates and question the importance of collagen as a critical extracellular matrix component for GBS infections of the central nervous system