H. Lindmark et B. Guss, SFS, a novel fibronectin-binding protein from Streptococcus equi, inhibitsthe binding between fibronectin and collagen, INFEC IMMUN, 67(5), 1999, pp. 2383-2388
The obligate parasitic bacterium Streptococcus equi subsp. equi is the caus
ative agent of strangles, a serious disease of the upper respiratory tract
in horses. In this study we have, using shotgun phage display, cloned from
S. equi subsp, equi and characterized a gene, called sfs, encoding a protei
n termed SFS, representing a new type of fibronectin (Fn)-binding protein,
The sfs gene was found to be present in all 50 isolates of S, equi subsp, e
qui tested and in 41 of 48 S, equi subsp, zooepidemicus isolates tested. Th
e sfs gene is down-regulated during growth in vitro compared to fnz, a prev
iously characterized gene encoding an Fn-binding protein from S. equi subsp
, zooepidemicus, Sequence comparisons revealed no similarities to previousl
y characterized Fn-binding proteins, but high scores were obtained against
collagen, Besides similarity due to the high content of glycine, serine, an
d proline residues present in both proteins, there was a nine-residue motif
present both in collagen and in the Fn-binding domain of SFS, By searching
the Oklahoma S. pyogenes database, we found that this motif is also presen
t in a potential cell surface protein from S. pyogenes, Protein SFS was fou
nd to inhibit the binding between Fn and collagen in a concentration-depend
ent way.