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

Shaynoor Dramsi (1) , Eric Morello (1) , Claire Poyart (2, 3) , Patrick Trieu-Cuot (1)

1 Biologie des Bactéries pathogènes à Gram-positif
2 Centre national de Référence des Streptocoques (CNR)
3 IC UM3 (UMR 8104 / U1016) - Institut Cochin

Group 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.

Domaines: Bactériologie

Shaynoor Dramsi, Eric Morello, Claire Poyart, Patrick Trieu-Cuot. Epidemiologically and clinically relevant Group B Streptococcus isolates do not bind collagen but display enhanced binding to human fibrinogen.. Microbes and infection / Institut Pasteur., 2012, 14 (12), pp.1044-8. ⟨10.1016/j.micinf.2012.07.004⟩. ⟨pasteur-01300174⟩