Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes.
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چکیده
منابع مشابه
Fibronectin binding to a Streptococcus pyogenes strain.
In previous studies, Staphylococcus aureus has been shown to bind fibronectin (P. Kuusela, Nature (London) 276:718-720, 1978), an interaction that may be important in bacterial attachment and opsonization. Recently some strains of streptococci of serological groups A, C, and G were also found to bind fibronectin. The binding to one selected strain of Streptococcus pyogenes has been characterize...
متن کاملStreptococcus pyogenes ( Group A Streptococcus )
Group A streptococcus (GAS) is synonymous with Streptococcus pyogenes, the only species within this group of β-hemolytic streptococci. GAS is one of the leading pathogenic bacteria that infects children and adolescents, and is associated with a wide spectrum of infections and disease states. Worldwide, there are estimated to be >600 million cases of GAS pharyngitis (“strep throat”) and >100 mil...
متن کاملProtein F, a fibronectin-binding protein of Streptococcus pyogenes, also binds human fibrinogen: isolation of the protein and mapping of the binding region.
During screening of a gene library of Streptococcus pyogenes type M15 for fibrinogen-binding material, a protein of approximately 100 kDa, encoded outside the vir region, was found. DNA sequencing revealed this component to be identical to protein F, a fibronectin-binding protein. Isolation of the recombinant protein, termed F15, was performed by the use of fibrinogen affinity chromatography. T...
متن کاملFc-mediated nonspecific binding between fibronectin-binding protein I of Streptococcus pyogenes and human immunoglobulins.
Fibronectin-binding protein I (SfbI) from Streptococcus pyogenes plays a key role in bacterial adhesion to, and invasion of, eukaryotic cells. In addition, SfbI exhibits a considerable potential as mucosal adjuvant and can trigger polyclonal activation of B cells. Here, we report that SfbI is also capable of binding human IgG in a nonimmune fashion. SfbI was reactive with IgG1, IgG2, IgG3, and ...
متن کاملExtended Binding Site on Fibronectin for the Functional Upstream Domain of Protein F1 of Streptococcus pyogenes*
The 49-residue functional upstream domain (FUD) of Streptococcus pyogenes F1 adhesin interacts with fibronectin (FN) in a heretofore unknown manner that prevents assembly of a FN matrix. Biotinylated FUD (b-FUD) bound to adsorbed FN or its recombinant N-terminal 70-kDa fibrin- and gelatin-binding fragment (70K). Binding was blocked by FN or 70K, but not by fibrin- or gelatin-binding subfragment...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1992
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.89.13.6172