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

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

Microbes and infection (2012-07-31)
Shaynoor Dramsi, Eric Morello, Claire Poyart, Patrick Trieu-Cuot
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Collagen Type IV from human cell culture, Bornstein and Traub Type IV, 0.3 mg/mL, sterile-filtered, BioReagent, suitable for cell culture
Sigma-Aldrich
Fibrinogen from human plasma, 50-70% protein (≥80% of protein is clottable)