• Publications
  • Influence
Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci
TLDR
Data suggest that FBP54 may be a surface protein of streptococci that reacts with both Fn and Fgn and therefore may participate in the adhesion of group A strePTococci to host cells. Expand
Molecular mechanisms of adhesion, colonization, and invasion of group A streptococci
TLDR
This review presents the different molecular mechanisms of adhesion utilized by group A streptococci and how these interactions lead to colonization and invasion. Expand
Serum opacity factor is a major fibronectin‐binding protein and a virulence determinant of M type 2 Streptococcus pyogenes
TLDR
Data clearly indicate that SOF is a virulence factor, and provide the first direct evidence that a fibronectin‐binding protein contributes to the pathogenesis of group A streptococcal infections in vivo. Expand
Multiple adhesins of streptococci
Human streptococcal isolates are confronted with numerous environmental challenges, one of which is the necessity that they adhere to one or more of the varied mucosal surfaces of the oropharyngealExpand
In vitro anti-bacterial and biological properties of magnetron co-sputtered silver-containing hydroxyapatite coating.
TLDR
The creation of a multifunctional surface can be achieved by co-sputtering the osteoconductive HA with antibacterial Ag with no significant difference in the in vitro cytotoxicty was observed between HA and Ag-HA surfaces. Expand
Quantitative differences in adhesiveness of type 1 fimbriated Escherichia coli due to structural differences in fimH genes
TLDR
The results presented here strongly suggest that the quantitative variations in MS adhesion are due primarily to structural differences in the FimH adhesin. Expand
Differential effects of the streptococcal fibronectin-binding protein, FBP54, on adhesion of group A streptococci to human buccal cells and HEp-2 tissue culture cells
TLDR
Data indicate that FBP54 is a streptococcal adhesin that is expressed in the human host and that preferentially mediates adhesion to certain types of human cells. Expand
Anti‐phagocytic mechanisms of Streptococcus pyogenes: binding of fibrinogen to M‐related protein
TLDR
Findings indicate that Mrp–fibrinogen interactions prevent surface deposition of complement via the classical pathway, thereby contributing to the ability of these streptococci to resist phagocytosis. Expand
Relationship between Expression of the Family of M Proteins and Lipoteichoic Acid to Hydrophobicity and Biofilm Formation in Streptococcus pyogenes
TLDR
The formation of complexes with members of the M protein family is a common mechanism for anchoring LTA on the surface in a manner that contributes to hydrophobicity and to biofilm formation in S. pyogenes, but these activities in some serotypes are dependent on a trypsin-sensitive protein(s). Expand
FimH family of type 1 fimbrial adhesins: functional heterogeneity due to minor sequence variations among fimH genes
TLDR
Evidence is provided that functional heterogeneity of type 1-fimbriated Escherichia coli strains CSH-50 and HB101(pPKL4), both K-12 derivatives, have different patterns of adhesion to yeast mannan, human plasma fibronectin, and fibronECTin derivatives, suggesting functional heterogeneity is due to variations in the fimH genes. Expand
...
1
2
3
4
5
...