scholarly journals Human Fibrinogen Inhibits Amyloid Assembly of Most Phenol-Soluble Modulins from Staphylococcus aureus

ACS Omega ◽  
2021 ◽  
Author(s):  
Zahra Najarzadeh ◽  
Janni Nielsen ◽  
Azad Farzadfard ◽  
Vita Sereikaite ◽  
Kristian Strømgaard ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Human Fibrinogen ◽  
Amyloid Assembly

Binding of staphylococcal cell surface polysaccharide to human fibrinogen

1990 ◽  
Vol 36 (3) ◽  
pp. 206-210
Author(s):  
Toshichika Ohtomo ◽  
Tsugiaki Kobayashi ◽  
Yukio Ohshima ◽  
Yukio Usui ◽  
Masaru Suganuma ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Surface ◽  
Binding Site ◽  
Key Words ◽  
Active Substance ◽  
Soft Agar ◽  
Alkaline Ph ◽  
Human Fibrinogen ◽  
Surface Polysaccharide ◽  
Alkaline Range

The interaction between the binding site of a polysaccharide (called compact colony forming active substance (CCFAS)), obtained from the cell surface of a strain of Staphylococcus, and human fibrinogen (HF) was investigated. The CCFAS was found to bind specifically to both the Bβ and γ chains of HF at pH 7.0 and 8.0, and the Aα chain at pH 5.0. The binding of CCFAS with fibrinogen fragments obtained by digestion with plasmin were also investigated. Fragments with Mr of 55 000, 24 000, and 19 000 were the major bands precipitated by CCFAS at pH 7.0 and 8.0. Fragments with Mr of 85 000 and 75 000 bound to CCFAS at pH 5.0. Binding of CCFAS (7 μg) with fibrinogen could be inhibited by 1.2 μg of Bβ chain and 1.5 μg γ chain at alkaline pH or 6.2 μg of the Aα chain at pH 5.0. CCFAS was, therefore, assumed to be specifically bonded with HF molecules, in the alkaline range at least, resulting in compact colony forming activity in serum soft agar and paracoagulation. Key words: cell surface, polysaccharide, Staphylococcus aureus, fibrinogen.

scholarly journals Anti-Clumping Factor A Immunoglobulin Reduces the Duration of Methicillin-Resistant Staphylococcus aureus Bacteremia in an Experimental Model of Infective Endocarditis

2003 ◽  
Vol 47 (11) ◽  
pp. 3400-3406 ◽  
Author(s):  
John Vernachio ◽  
Arnold S. Bayer ◽  
Thuan Le ◽  
Yin-Li Chai ◽  
Bradley Prater ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Infective Endocarditis ◽  
Combination Therapy ◽  
Rabbit Model ◽  
Human Fibrinogen ◽  
Methicillin Resistant ◽  
Staphylococcus Aureus Bacteremia ◽  
Fibrinogen Binding ◽  
Human Polymorphonuclear Leukocytes

ABSTRACT SA-IGIV is a human polyclonal immunoglobulin containing elevated levels of antibodies specific for the fibrinogen-binding MSCRAMM protein clumping factor A (ClfA). In vitro, SA-IGIV specifically recognized ClfA that was expressed on the surface of Staphylococcus aureus and inhibited bacterial adherence to immobilized human fibrinogen by >95%. Moreover, SA-IGIV efficiently opsonized ClfA-coated fluorescent beads and facilitated phagocytosis by human polymorphonuclear leukocytes. To determine its potential therapeutic efficacy, SA-IGIV was evaluated in combination with vancomycin in a rabbit model of catheter-induced aortic valve infective endocarditis (IE) caused by methicillin-resistant S. aureus (MRSA). The combination therapy was more effective than vancomycin alone in sterilizing all valvular vegetations when used therapeutically during early (12-h) IE. The combination therapy resulted in clearance of bacteremia that was significantly faster than that of vancomycin alone in animals with well-established (24-h) IE. Therefore, in both early and well-established MRSA IE, the addition of SA-IGIV to a standard antibiotic regimen (vancomycin) increased bacterial clearance from the bloodstream and/or vegetations.

scholarly journals Identification of the Staphylococcus aureus MSCRAMM clumping factor B (ClfB) binding site in the αC-domain of human fibrinogen

Microbiology ◽  
2008 ◽  
Vol 154 (2) ◽  
pp. 550-558 ◽  
Author(s):  
Evelyn J. Walsh ◽  
Helen Miajlovic ◽  
Oleg V. Gorkun ◽  
Timothy J. Foster
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Site ◽  
Human Fibrinogen ◽  
Factor B ◽  
Clumping Factor B

Human Fibrinogen Inhibits Amyloid Assembly of Biofilm-Forming CsgA

Biochemistry ◽  
2018 ◽  
Vol 57 (44) ◽  
pp. 6270-6273 ◽  
Author(s):  
Hema M. Swasthi ◽  
Karishma Bhasne ◽  
Sayanta Mahapatra ◽  
Samrat Mukhopadhyay
Keyword(s):  
Human Fibrinogen ◽  
Amyloid Assembly

scholarly journals Characterization of a Protective Monoclonal AntibodyRecognizing Staphylococcus aureus MSCRAMM ProteinClumping FactorA

2003 ◽  
Vol 71 (12) ◽  
pp. 6864-6870 ◽  
Author(s):  
Andrea E. Hall ◽  
Paul J. Domanski ◽  
Pratiksha R. Patel ◽  
John H. Vernachio ◽  
Peter J. Syribeys ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Flow Cytometric Analysis ◽  
Experimental Models ◽  
In Vivo Evaluation ◽  
Human Fibrinogen ◽  
Treatment And Prevention ◽  
Flow Cytometric ◽  
Life Threatening

ABSTRACT The Staphylococcus aureus MSCRAMM (microbial surface components recognizing adhesive matrix molecules) protein clumping factor A (ClfA) has been shown to be a critical virulence factor in several experimental models of infection. This report describes the generation, characterization, and in vivo evaluation of a murine monoclonal antibody (MAb) against ClfA. Flow cytometric analysis revealed that MAb 12-9 recognized ClfA protein expressed by all of the clinical S. aureus strains obtained from a variety of sources. In assays measuring whole-cell S. aureus binding to human fibrinogen, MAb 12-9 inhibited S. aureus binding by over 90% and displaced up to 35% of the previously adherent S. aureus bacteria. Furthermore, a single infusion of MAb 12-9 was protective against an intravenous challenge with a methicillin-resistant strain of S. aureus in a murine sepsis model (P< 0.0001). These data suggest that anti-ClfA MAb 12-9 should be further investigated as a novel immunotherapy for the treatment and prevention of life-threatening S. aureus infections.

Cytochemical Studies of Cell Wall Biosynthesis in Staphylococcus Aureus

1972 ◽  
Vol 30 ◽  
pp. 328-329
Author(s):  
Masaatsu Koike ◽  
Koichi Nakashima ◽  
Kyoko Iida
Keyword(s):  
Staphylococcus Aureus ◽  
Periodate Oxidation ◽  
Early Time ◽  
The Other ◽  
Penicillin G ◽  
Cell Wall Biosynthesis ◽  
Septal Wall ◽  
Peptidoglycan Biosynthesis ◽  
Gram Positive Bacteria ◽  
Cross Linkage

Penicillin exerts the activity to inhibit the peptide cross linkage between each polysaccharide backbone at the final stage of wall-peptidoglycan biosynthesis of bacteria. Morphologically, alterations of the septal wall and mesosome in gram-positive bacteria, which were occurred in early time after treatment with penicillin, have been observed. In this experiment, these alterations were cytochemically investigated by means of silver-methenamine staining after periodate oxidation, which is applied for detection of localization of wall mucopolysaccharide.Staphylococcus aureus strain 209P treated with 100 u/ml of penicillin G was divided into two aliquotes. One was fixed by Kellenberger-Ryter's OSO4 fixative at 30, 60 and 120 min after addition of the antibiotic, dehydrated through alcohol series, and embedded in Epon 812 (Specimen A). The other was fixed by 21 glutaraldehyde, dehydrated through glycolmethacrylate series and embedded in glycolmethacrylate mixture, according to Bernhard's method (Specimen B).

Gold labeling of teichoic acid on adjacent surfaces of staphylococcus aureus

1990 ◽  
Vol 48 (3) ◽  
pp. 578-579
Author(s):  
Margaret Hukee
Keyword(s):  
Staphylococcus Aureus ◽  
Teichoic Acid ◽  
Protein Labeling ◽  
Minimal Amount ◽  
Section Thickness ◽  
Double Labeling ◽  
Parallel Surfaces ◽  
Supporting Membrane

Gold labeling of two antigens (double labeling) is often done on two section surfaces separated by section thickness. Whether labeling is done on both sides of the same section or on two parallel surfaces separated by section thickness (PSSST), comparable results are dependent on an equal number of epitopes being exposed at each surface. We propose a method to study protein labeling within the same field of proteins, by examining two directly adjacent surfaces that were split during sectioning. The number of labeling sites on adjacent surfaces (AS) were compared to sites on PSSST surfaces in individual bacteria.Since each bacteria needed to be recognizable in all three section surfaces, one-hole grids were used for labeling. One-hole grids require a supporting membrane and excessive handling during labeling often ruptures the membrane. To minimize handling, a labeling chamber was designed that is inexpensive, disposable, minimizes contamination, and uses a minimal amount of solution.

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