title: Epidemiologically and clinically relevant Group B Streptococcus isolates do not bind collagen but display enhanced binding to human fibrinogen.
abstract: 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.
authors: Institut Pasteur, Unité des Bactéries Pathogènes à Gram positif, 75015 Paris, France. shaynoor.dramsi@pasteur.fr
authors: Shaynoor
authors: S
authors: Dramsi
authors: Eric
authors: E
authors: Morello
authors: Claire
authors: C
authors: Poyart
authors: Patrick
authors: P
authors: Trieu-Cuot
mesh_terms: D001422:Bacterial Adhesion; D003094:Collagen / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D013292:Streptococcus agalactiae / Q000472:pathogenicity* / Q000502:physiology
chemical_list: D005340:Fibrinogen; D003094:Collagen