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Infect. Immun., 04 1997, 1357-1363, Vol 65, No. 4
G Molinari, SR Talay, P Valentin-Weigand, M Rohde and GS Chhatwal
Streptococcus pyogenes organisms (group A streptococci) are considered to
be highly adhesive extracellular pathogens. However, it has recently been
reported that S. pyogenes has the capacity to efficiently invade eukaryotic
cells. In this study, we demonstrate that the interaction of S. pyogenes
fibronectin-binding protein (SfbI) with fibronectin on nonphagocytic HEp-2
cells triggers bacterial internalization. Blocking of the SfbI adhesin by
either antibodies against the whole protein or antibodies against the
fibronectin-binding domains of SfbI, as well as pretreatment of HEp-2 cells
with purified SfbI protein, prevents both S. pyogenes attachment and
internalization. Inert latex beads precoated with the purified SfbI protein
are ingested by eukaryotic cells, demonstrating that SfbI is per se enough
to trigger the internalization process. Experiments performed with a
recombinant SfbI domain encompassing the two fibronectin-binding regions of
the SfbI molecule demonstrated that these binding regions are essential and
sufficient to activate uptake by HEp-2 cells. These results demonstrate
that the fibronectin-binding protein SfbI is involved in both S. pyogenes'
attachment to and ingestion by HEp-2 cells and contribute to elucidation of
the underlying molecular events leading to eukaryotic cell invasion by S.
pyogenes.
Copyright © 1997, American Society for Microbiology
The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells
Division of Microbiology, Technical University/GBF-National Research Centre for Biotechnology, Braunschweig, Germany. gmo@gbf-braunschweig.de
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