A 28-kilodalton fibronectin-binding protein of group a streptococci

1992 ◽  
Vol 25 (5) ◽  
pp. 245-250 ◽  
Author(s):  
Harry S. Courtney ◽  
David L. Hasty ◽  
James B. Dale ◽  
Thomas P. Poirier
Keyword(s):  
Binding Protein ◽  
Group A Streptococci ◽  
Group A ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

scholarly journals Identification and Characterization of a Novel Fibronectin-Binding Protein on the Surface of Group A Streptococci

1999 ◽  
Vol 67 (6) ◽  
pp. 2720-2728 ◽  
Author(s):  
Claudia L. Rocha ◽  
Vincent A. Fischetti
Keyword(s):  
Cell Growth ◽  
Binding Proteins ◽  
Genomic Library ◽  
Binding Protein ◽  
Terminal Region ◽  
Group A Streptococci ◽  
Gram Positive ◽  
Group A ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

ABSTRACT Understanding the role surface proteins play in the interaction of group A streptococci with epithelial cells is an important step toward the development of new strategies to fight infections. Fibronectin-binding proteins in streptococci and staphylococci have been described as important mediators for adherence to eukaryotic cells. In the present study we describe a new Streptococcus pyogenes fibronectin-binding protein (PFBP). The gene encoding the PFBP protein (pfbp) was identified from an M12 strain genomic library. It encodes a protein of 127.4 kDa which contains the LPXTGX motif characteristic of cell wall-associated proteins in gram-positive organisms and is among the largest surface molecules described for group A streptococci. The pfbp gene is transcribed during cell growth and was present in several class I and II streptococcal strains tested. The deduced amino acid sequence of PFBP exhibits a variable N-terminal region and a conserved C-terminal region when compared to most fibronectin-binding proteins identified from other gram-positive bacteria. The N-terminal region presents a stretch of 105 amino acids with no homology with N-terminal regions of previously described fibronectin-binding molecules, while the C-terminal region contains three repeat domains that share significant similarity with the repeat regions of fibronectin-binding proteins fromS. pyogenes, S. dysgalactiae, and S. equisimilis. The PFBP repeated region, when expressed on the surface of S. gordonii, a commensal organism, binds to soluble and immobilized fibronectin. This study also shows that, in addition to pfbp, a second gene homologous with that of protein F1 (which also codes for a fibronectin-binding protein) is transcribed during cell growth in the same S. pyogenesstrain.

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.

scholarly journals Fibronectin-Binding Protein Gene Recombination and Horizontal Transfer between Group A and G Streptococci

2004 ◽  
Vol 42 (11) ◽  
pp. 5357-5361 ◽  
Author(s):  
R. J. Towers ◽  
D. Gal ◽  
D. McMillan ◽  
K. S. Sriprakash ◽  
B. J. Currie ◽  
...  
Keyword(s):  
Horizontal Transfer ◽  
Protein Gene ◽  
Binding Protein ◽  
Gene Recombination ◽  
Group A ◽  
Fibronectin Binding Protein ◽  
Binding Protein Gene ◽  
Fibronectin Binding

scholarly journals Distribution and Antigenicity of Fibronectin Binding Proteins (SfbI and SfbII) of Streptococcus pyogenes Clinical Isolates from the Northern Territory, Australia

2000 ◽  
Vol 38 (1) ◽  
pp. 389-392
Author(s):  
Alison M. Goodfellow ◽  
Megan Hibble ◽  
Susanne R. Talay ◽  
Bernd Kreikemeyer ◽  
Bart J. Currie ◽  
...  
Keyword(s):  
Streptococcus Pyogenes ◽  
Immunoglobulin G ◽  
Binding Proteins ◽  
Northern Territory ◽  
Clinical Isolates ◽  
Group A Streptococci ◽  
Streptococcal Infections ◽  
Group A ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

ABSTRACT Fibronectin binding proteins play an important role in the adherence and invasion of group A streptococci (GAS). Genotypically distinct GAS isolates were screened for the presence and expression of two streptococcal fibronectin binding protein genes, sfbI and sfbII . Of the tested strains, 64 and 36% were shown to harbor and express the sfbI and sfbII genes, respectively. All sfbII -positive strains tested were also positive for sfbI , but only 28% of the sfbII -negative strains were positive for sfbI . High levels of immunoglobulin G antibodies to both SfbI and SfbII were found in sera from 80 subjects with defined streptococcal infections.

scholarly journals Molecular Genetic Analysis of a Group A Streptococcus Operon Encoding Serum Opacity Factor and a Novel Fibronectin-Binding Protein, SfbX

2003 ◽  
Vol 185 (4) ◽  
pp. 1208-1217 ◽  
Author(s):  
Arthur Jeng ◽  
Varja Sakota ◽  
Zhongya Li ◽  
Vivekananda Datta ◽  
Bernard Beall ◽  
...  
Keyword(s):  
Group A Streptococcus ◽  
Binding Protein ◽  
Molecular Genetic ◽  
Transcription Unit ◽  
Molecular Genetic Analysis ◽  
Serum Opacity Factor ◽  
Group A ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding ◽  
Classical Association

ABSTRACT The group A Streptococcus (GAS) sof gene encodes the serum opacity factor protein, which is capable of opacifying mammalian sera and binding at least two host proteins, fibronectin and fibrinogen. The sof gene exists in approximately 50% of clinical isolates, and there is a classical association of so-called nephritogenic strains with the opacity factor-positive phenotype. In both a type emm49 strain and a type emm12 strain, the sequences upstream of the 5′ end of sof and downstream of the putative terminator were determined to be nearly identical to a region in the M type 1 genome approximately 10 kb upstream of the emm1 gene. This close genetic linkage is likely reflected in the strict correlation of opacity factor phenotype with specific emm genotypes. A new fibronectin-binding protein gene, sfbX, was discovered immediately downstream of sof in emm12 and emm49 strains and in several other sof-positive strains. The sof and sfbX genes were found to be expressed on the same transcription unit, which was correlated with the putative promoter and rho-independant terminator sequences that flank these two genes. The sfbX genes from different emm types are predicted to encode ∼650-residue surface-bound proteins sharing 89 to 92% sequence identity. SfbX residues approximately 1 to 480 are not highly similar to those of other known proteins, with the closest match being the Staphylococcus aureus coagulase protein. The remaining portions of these proteins (residues 481 to 650) contain four putative fibronectin-binding repeats highly similar to those of other streptococcal fibronectin-binding proteins and a potential LP(X)SG cell wall anchor motif. Targeted in-frame allelic-exchange mutagenesis, complementation, and heterologous-expression studies found that serum opacification is encoded by sof alone and that sfbX encodes a fibronectin-binding function. A recombinant SfbX protein was found to bind immobilized fibronectin and to partially inhibit GAS adherence to fibronectin. The sfbX gene was found to be present only in sof-positive strains, and together these genes could influence the spectrum of tissues colonized by sof-positive GAS.

scholarly journals Intranasal Vaccination with Streptococcal Fibronectin Binding Protein Sfb1 Fails To Prevent Growth and Dissemination of Streptococcus pyogenes in a Murine Skin Infection Model

2004 ◽  
Vol 72 (12) ◽  
pp. 7342-7345 ◽  
Author(s):  
J. McArthur ◽  
E. Medina ◽  
A. Mueller ◽  
J. Chin ◽  
B. J. Currie ◽  
...  
Keyword(s):  
Streptococcus Pyogenes ◽  
Skin Infection ◽  
Group A Streptococcus ◽  
Binding Protein ◽  
Infection Model ◽  
Cholera Toxin B Subunit ◽  
Protective Antigens ◽  
Group A ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

ABSTRACT Fibronectin binding protein F1 (Sfb1) of Streptococcus pyogenes (group A streptococcus [GAS]) is a well-characterized adhesin that has been shown to induce protection in mice against a lethal intranasal GAS challenge after intranasal immunization with cholera toxin B subunit (CTB) as adjuvant. With a murine skin infection model, we have shown that Sfb1/CTB vaccination neither elicits opsonizing antibodies nor prevents systemic bacterial growth and dissemination to internal organs after a subcutaneous GAS challenge. These results indicate that an Sfb1-based vaccine should be complemented with additional protective antigens in order to be used in areas such as the tropical north of Australia, where the skin is the primary route of entry for invasive streptococcal diseases.

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