Inhibition of sortase-mediated Staphylococcus aureus adhesion to fibronectin via fibronectin-binding protein by sortase inhibitors

2006 ◽  
Vol 70 (1) ◽  
pp. 102-106 ◽  
Author(s):  
Ki-Bong Oh ◽  
Mi-Na Oh ◽  
Jae-Gyu Kim ◽  
Dong-Sun Shin ◽  
Jongheon Shin
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Protein ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

scholarly journals Fibronectin-binding protein B variation in Staphylococcus aureus

2010 ◽  
Vol 10 (1) ◽  
pp. 160 ◽  
Author(s):  
Fiona M Burke ◽  
Niamh McCormack ◽  
Simonetta Rindi ◽  
Pietro Speziale ◽  
Timothy J Foster
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Protein ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding ◽  
Protein B

scholarly journals Molecular Investigation of Fibronectin-Binding Protein Genes and Capacity of Biofilm Production in Staphylococcus Aureus Isolated From Clinical Samples

2021 ◽  
Author(s):  
Hossein Jafari Soghondicolaei ◽  
Mohammad Ahanjan ◽  
Mehrdad Gholami ◽  
Bahman Mirzaei ◽  
Hamid Reza Goli
Keyword(s):  
Staphylococcus Aureus ◽  
Biofilm Formation ◽  
Colorimetric Assay ◽  
Binding Protein ◽  
Clinical Isolates ◽  
Diffusion Method ◽  
Clinical Samples ◽  
Biofilm Production ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

Abstract Biofilm production increases Staphylococcus aureus resistance to antibiotics and also host defense mechanisms. The current study aims to evaluate the biofilm formation by S. aureus and to determine the prevalence of fibronectin-binding protein genes, also its correlation with drug resistance. In this study, 100 clinical isolates of S. aureus were collected. The antibiotic susceptibility pattern of the isolates was evaluated by the disk agar diffusion method. The ability of biofilm formation in the studied isolates was also determined by microplate colorimetric assay. Then, all isolates were screened by polymerase chain reaction for the fnbA and fnbB genes. Out of 100 clinical isolates of S. aureus, the highest and lowest antibiotic resistance rates were against penicillin (94%) and vancomycin (6%). Thirty-two cases were found to be multi-drug resistant (MDR) among the all strains. The ability of biofilm production was observed in 89% of the isolates. The PCR results showed that the prevalence of fnbA and fnbB genes were 91% and 17%, respectively. Moreover, 100% and 21.8% of the MDR strains harbored the fnbA and fnbB genes respectively. The ability to form biofilm in MDR isolates of S. aureus is more than non-MDR isolates, especially fnbA positive ones. As the bacteria in the biofilm are difficult to kill by antibiotics, attention to the removal or control of the biofilm production seems to be necessary.

scholarly journals Prevalence and distribution of adhesins and the expression of fibronectin-binding protein (FnbA and FnbB) among Staphylococcus aureus isolates from Shahrekord Hospitals

2019 ◽  
Vol 12 (1) ◽  
Author(s):  
Emad Soltani ◽  
Effat Farrokhi ◽  
Behnam Zamanzad ◽  
Milad Shahini Shams Abadi ◽  
Fatemeh Deris ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Protein ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

scholarly journals Increased Virulence of a Fibronectin-Binding Protein Mutant of Staphylococcus aureus in a Rat Model of Pneumonia

2002 ◽  
Vol 70 (7) ◽  
pp. 3865-3873 ◽  
Author(s):  
Mary C. McElroy ◽  
David J. Cain ◽  
Christine Tyrrell ◽  
Timothy J. Foster ◽  
Christopher Haslett
Keyword(s):  
Staphylococcus Aureus ◽  
Epithelial Cells ◽  
Rat Model ◽  
Binding Proteins ◽  
Binding Protein ◽  
Alveolar Epithelial Cells ◽  
Alveolar Epithelial ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

ABSTRACT Fibronectin-binding proteins mediate Staphylococcus aureus internalization into nonphagocytic cells in vitro. We have investigated whether fibronectin-binding proteins are virulence factors in the pathogenesis of pneumonia by using S. aureus strain 8325-4 and isogenic mutants in which fibronectin-binding proteins were either deleted (DU5883) or overexpressed [DU5883(pFnBPA4)]. We first demonstrated that fibronectin-binding proteins mediate S. aureus internalization into alveolar epithelial cells in vitro and that S. aureus internalization into alveolar epithelial cells requires actin rearrangement and protein kinase activity. Second, we established a rat model of S. aureus-induced pneumonia and measured lung injury and bacterial survival at 24 and 96 h postinoculation. S. aureus growth and the extent of lung injury were both increased in rats inoculated with the deletion mutant (DU5883) in comparison with rats inoculated with the wild-type (8325-4) and the fibronectin-binding protein-overexpressing strain DU5883(pFnBPA4) at 24 h postinfection. Morphological evaluation of infected lungs at the light and electron microscopic levels demonstrated that S. aureus was present within neutrophils from both 8325-4- and DU5883-inoculated lungs. Our data suggest that fibronectin-binding protein-mediated internalization into alveolar epithelial cells is not a virulence mechanism in a rat model of pneumonia. Instead, our data suggest that fibronectin-binding proteins decrease the virulence of S. aureus in pneumonia.

Adherence of Staphylococcus aureus fibronectin binding protein A mutants: an investigation using optical tweezers

2004 ◽  
Vol 21 (3-5) ◽  
pp. 105-111 ◽  
Author(s):  
Kathryn H. Simpson ◽  
M. Gabriela Bowden ◽  
Sharon J. Peacock ◽  
Maneesh Arya ◽  
Magnus Höök ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Optical Tweezers ◽  
Binding Protein ◽  
Protein A ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

scholarly journals Specific T cells targeting Staphylococcus aureus Fibronectin‐binding protein 1 induce a type 2/type 1 inflammatory response in sensitized atopic dermatitis patients

Allergy ◽  
2021 ◽  
Author(s):  
Ahmed K. Farag ◽  
Lennart M. Roesner ◽  
Susanne Wieschowski ◽  
Annice Heratizadeh ◽  
Britta Eiz‐Vesper ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
T Cells ◽  
Atopic Dermatitis ◽  
Inflammatory Response ◽  
Binding Protein ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding
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