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Localization and characterization of fibronectin-binding to group A streptococci. An electron microscopic study using
B Wagner1, K H Schmidt, M Wagner
1Central Institute of Microbiology and Experimental Therapy, Academy of Sciences of the GDR, Jena.
Abstract:
The location and nature of the binding sites for fibronectin (Fn) and its N-terminal 29 K fragment (FnF) on group A streptococci were studied by electron microscopy using these proteins labelled with colloidal gold. The investigated strains exhibited a different labelling intensity as well as a different labelling pattern varying from a strong regular distribution to a weak focal binding. Binding of Fn and FnF was inhibited by itself as well as by lipoteichoic acid (LTA), anti-LTA and concanavalin A. Simultaneous labelling of the bacteria with marker complexes of FnF, human serum albumin and fibrinogen revealed separate receptor sites for each protein. Our results confirmed LTA to be mainly responsible for the binding of Fn on group A streptococci.