Inhibition of Streptococcus pyogenes adherence to HaCaT cells by a peptide corresponding to the streptococcal fibronectin-binding protein, SfbI, is strain dependent

2004 ◽  
Vol 6 (10) ◽  
pp. 926-928 ◽  
Author(s):  
Mandy L. Edwards ◽  
Peter K. Fagan ◽  
Rebecca J. Towers ◽  
Bart J. Currie ◽  
Kadaba S. Sriprakash
Keyword(s):  
Streptococcus Pyogenes ◽  
Binding Protein ◽  
Hacat Cells ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding ◽  
Strain Dependent ◽  
Is Strain

scholarly journals Association between Resistance to Erythromycin and the Presence of the Fibronectin Binding Protein F1 Gene, prtF1, in Streptococcus pyogenes Isolates from German Pediatric Patients

2005 ◽  
Vol 49 (7) ◽  
pp. 2990-2993 ◽  
Author(s):  
Maria Haller ◽  
Kirsten Fluegge ◽  
Sandra Jasminder Arri ◽  
Brit Adams ◽  
Reinhard Berner
Keyword(s):  
Streptococcus Pyogenes ◽  
Pediatric Patients ◽  
Group A Streptococcus ◽  
Binding Protein ◽  
Macrolide Resistance ◽  
Group A ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding ◽  
Cell Invasiveness

ABSTRACT A total of 301 German pediatric group A streptococcus isolates were screened for the presence of macrolide resistance and the fibronectin binding protein F1 gene (prtF1) encoding an adhesin and cell invasiveness protein. The prtF1 gene was present significantly more often among macrolide-resistant isolates. The majority of these were not clonally related.

Streptococcus pyogenes Fibronectin-Binding Protein Is a Novel Prothrombin Activator.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 1691-1691
Author(s):  
Jonathan I. Creamer ◽  
Peter R. Panizzi ◽  
Paul E. Bock
Keyword(s):  
Fusion Protein ◽  
Streptococcus Pyogenes ◽  
Active Site ◽  
Binding Protein ◽  
Catalytic Site ◽  
Fluorescence Probes ◽  
Binding Studies ◽  
Human Fibrinogen ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

Abstract Streptococcus pyogenes fibronectin-binding Protein (SfbX), expressed by emm12 and emm49 strains of S. pyogenes, binds fibronectin through COOH-terminal interactions of the protein.1 SfbX NH2-terminal residues 54–229 share 21% identity to staphylocoagulase (SC) residues 107–321 from Tager 104 strain, which increases to 35% homology when conservative substitutions are considered. SC is a non-proteolytic activator of the central coagulation zymogen prothrombin (ProT). Our structure of the prethrombin 2 complex with a fully active SC fragment (SC(1-325)) showed that SC(1-325) consisted of two α-helical bundle domains and that the NH2-terminal dipeptide is critical for ProT activation via the molecular sexuality mechanism.2 In this mechanism, SC inserts its NH2-terminal Ile1 into the Asp194 pocket of the ProT catalytic domain, inducing conformational activation of the catalytic site. On the basis of its homology, SfbX has been postulated to be a member of the SC family of zymogen activator and adhesion proteins. Plasmids encoding a His6-tagged SfbX(1-312) tobacco etch virus proteinase-cleavable fusion protein and the viral proteinase were co-transformed into E. coli to enable generation of the native SfbX NH2-terminus (Ile-Ser-Asn) during purification. SfbX(1-312) was purified by affinity chromatography on ProT-Affigel and Ni2+-iminodiacetic acid-Sepharose. Active site-specific fluorescent probe labeling of a mixture of ProT and SfbX(1-312) showed covalent labeling of the ProT zymogen, demonstrating that SfbX(1-312) is a non-proteolytic activator of ProT. Incubation of ProT with the NH2-terminally blocked SfbX(1-312) fusion protein did not result in labeling of the active site, indicating that the native NH2-terminus is required for activation, and suggesting that SfbX(1-312) activates ProT through the molecular sexuality mechanism. In ProT activation assays measured by the appearance of chromogenic substrate activity, SfbX(1-312) activated ProT weakly and was more effective in activating prethrombin 1, lacking the fragment 1 domain of ProT. Preliminary binding studies using ProT and thrombin labeled at the catalytic site with fluorescence probes demonstrated binding of SfbX(1-312). SfbX(1-312) decreased thrombin activity toward D-Phe-Pip-Arg-pNA by 75%, with an apparent KD of ~20 nM, indicating that the thrombin catalytic site is perturbed by SfbX binding. Clotting assays showed that neither SfbX(1-312) nor a mixture of SfbX(1-312) and prethrombin 1 clotted human fibrinogen or plasma. Addition of 5 μM SfbX(1-312) to a factor V-dependent plasma clotting assay increased clotting times, indicating that SfbX(1-312) has an inhibitory effect. We conclude that SfbX(1-312) activates ProT conformationally, possibly through the molecular sexuality mechanism. SfbX(1-312) binds tightly to thrombin, perturbing its catalytic site, but does not clot human fibrinogen or plasma. Further studies are needed to determine whether ProT is the pathophysiological target zymogen of SfbX(1-312), to delineate the natural substrate of the SfbX(1-312)·ProT complex, and to elucidate the role of SfbX in the pathology of S. pyogenes infection.

Identification of a Fibronectin-Binding Protein as Adhesin of Streptococcus pyogenes

1993 ◽  
Vol 278 (2-3) ◽  
pp. 238-245 ◽  
Author(s):  
Peter Valentin-Weigand ◽  
Susanne R. Talay ◽  
Kenneth N. Timmis ◽  
Gursharan S. Chhatwal
Keyword(s):  
Streptococcus Pyogenes ◽  
Binding Protein ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

Protein F2, a novel fibronectin‐binding protein from Streptococcus pyogenes , possesses two binding domains

1996 ◽  
Vol 21 (2) ◽  
pp. 373-384 ◽  
Author(s):  
Joseph Jaffe ◽  
Shira Natanson‐Yaron ◽  
Michael G. Caparon ◽  
Emanuel Hanski
Keyword(s):  
Streptococcus Pyogenes ◽  
Binding Protein ◽  
Binding Domains ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

scholarly journals Systemic and Mucosal Immunizations with Fibronectin-Binding Protein FBP54 Induce Protective Immune Responses against Streptococcus pyogenes Challenge in Mice

2001 ◽  
Vol 69 (2) ◽  
pp. 924-930 ◽  
Author(s):  
Shigetada Kawabata ◽  
Eiji Kunitomo ◽  
Yutaka Terao ◽  
Ichiro Nakagawa ◽  
Ken Kikuchi ◽  
...  
Keyword(s):  
Streptococcus Pyogenes ◽  
Binding Protein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Igg Antibodies ◽  
Igg Antibody ◽  
Antibody Titers ◽  
Fibronectin Binding Protein ◽  
Specific Igg ◽  
Fibronectin Binding ◽  
Specific Igg Antibodies

ABSTRACT The purpose of this study was to examine the suitability of fibronectin-binding protein FBP54 as a putative vaccine forStreptococcus pyogenes infections. When the distribution of the fbp54 gene among the clinical isolates representing various M serotypes was tested by PCR and Southern blot assays, it was found that all of the strains possess this gene. Furthermore, a significant increase in immunoglobulin G (IgG) antibody titers against FBP54 was observed in sera from patients with S. pyogenesinfections compared with those from healthy volunteers (P < 0.005). Mice were immunized with FBP54 subcutaneously, orally, or nasally. An enzyme-linked immunosorbent assay revealed that antigen-specific IgG antibodies were induced in the sera of immunized mice, while high salivary levels of IgA antibodies were detected after oral and nasal immunizations. Mice subcutaneously or orally immunized with FBP54 survived significantly longer following the challenge with S. pyogenes than did nonimmunized mice (P < 0.001). These results indicate that FBP54 is a promising vaccine for the prevention of S. pyogenesinfections.

scholarly journals Serum opacity factor is a major fibronectin-binding protein and a virulence determinant of M type 2 Streptococcus pyogenes

1999 ◽  
Vol 32 (1) ◽  
pp. 89-98 ◽  
Author(s):  
Harry S. Courtney ◽  
David L. Hasty ◽  
Yi Li ◽  
Herbert C. Chiang ◽  
Jenny L. Thacker ◽  
...  
Keyword(s):  
Streptococcus Pyogenes ◽  
Binding Protein ◽  
Virulence Determinant ◽  
Serum Opacity Factor ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

Fibronectin binding protein genes and cell invasion ability of Streptococcus pyogenes isolated from different sources

2006 ◽  
Vol 1289 ◽  
pp. 243-245 ◽  
Author(s):  
L. Baldassarri ◽  
S. Recchia ◽  
M. Imperi ◽  
R. Creti ◽  
G. Alfarone ◽  
...  
Keyword(s):  
Streptococcus Pyogenes ◽  
Cell Invasion ◽  
Binding Protein ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding ◽  
Different Sources
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