Streptococcal Opacity Factor: A Family of Bifunctional Proteins with Lipoproteinase and Fibronectin-Binding Activities

2000 ◽  
Vol 40 (3) ◽  
pp. 149-156 ◽  
Author(s):  
Viacheslav Katerov ◽  
Per-Erik Lindgren ◽  
Artem A. Totolian ◽  
Claes Schalén
Keyword(s):  
Bifunctional Proteins ◽  
Fibronectin Binding

Functional Characterization of PM6/13, a β3-specific (GPIIIa/CD61) Monoclonal Antibody that Shows Preferential Inhibition of Fibrinogen Binding over Fibronectin Binding to Activated Human Platelets

1998 ◽  
Vol 79 (01) ◽  
pp. 177-185 ◽  
Author(s):  
Ashia Siddiqua ◽  
Michael Wilkinson ◽  
Vijay Kakkar ◽  
Yatin Patel ◽  
Salman Rahman ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Platelet Aggregation ◽  
Platelet Rich Plasma ◽  
Functional Characterization ◽  
Human Platelets ◽  
Western Blots ◽  
Activated Platelets ◽  
Reducing Conditions ◽  
Fibronectin Binding

SummaryWe report the characterization of a monoclonal antibody (MAb) PM6/13 which recognises glycoprotein IIIa (GPIIIa) on platelet membranes and in functional studies inhibits platelet aggregation induced by all agonists examined. In platelet-rich plasma, inhibition of aggregation induced by ADP or low concentrations of collagen was accompanied by inhibition of 5-hydroxytryptamine secretion. EC50 values were 10 and 9 [H9262]g/ml antibody against ADP and collagen induced responses respectively. In washed platelets treated with the cyclooxygenase inhibitor, indomethacin, PM6/13 inhibited platelet aggregation induced by thrombin (0.2 U/ml), collagen (10 [H9262]g/ml) and U46619 (3 [H9262]M) with EC50 = 4, 8 and 4 [H9262]g/ml respectively, without affecting [14C]5-hydroxytryptamine secretion or [3H]arachidonate release in appropriately labelled cells. Studies in Fura 2-labelled platelets revealed that elevation of intracellular calcium by ADP, thrombin or U46619 was unaffected by PM6/13 suggesting that the epitope recognised by the antibody did not influence Ca2+ regulation. In agreement with the results from the platelet aggregation studies, PM6/13 was found to potently inhibit binding of 125I-fibrinogen to ADP activated platelets. Binding of this ligand was also inhibited by two other MAbs tested, namely SZ-21 (also to GPIIIa) and PM6/248 (to the GPIIb-IIIa complex). However when tested against binding of 125I-fibronectin to thrombin stimulated platelets, PM6/13 was ineffective in contrast with SZ-21 and PM6/248, that were both potent inhibitors. This suggested that the epitopes recognised by PM6/13 and SZ-21 on GPIIIa were distinct. Studies employing proteolytic dissection of 125I-labelled GPIIIa by trypsin followed by immunoprecipitation with PM6/13 and analysis by SDS-PAGE, revealed the presence of four fragments at 70, 55, 30 and 28 kDa. PM6/13 did not recognize any protein bands on Western blots performed under reducing conditions. However Western blotting analysis with PM6/13 under non-reducing conditions revealed strong detection of the parent GP IIIa molecule, of trypsin treated samples revealed recognition of an 80 kDa fragment at 1 min, faint recognition of a 60 kDa fragment at 60 min and no recognition of any product at 18 h treatment. Under similar conditions, SZ-21 recognized fragments at 80, 75 and 55 kDa with the 55kDa species persisting even after 18 h trypsin treatment. These studies confirm the epitopes recognised by PM6/13 and SZ-21 to be distinct and that PM6/13 represents a useful tool to differentiate the characteristics of fibrinogen and fibronectin binding to the GPIIb-IIIa complex on activated platelets.

Fibronectin binding to glomerular basement membrane is altered in diabetes

Diabetes ◽  
1987 ◽  
Vol 36 (6) ◽  
pp. 758-763 ◽  
Author(s):  
M. P. Cohen ◽  
R. Saini ◽  
H. Klepser ◽  
L. G. Vasanthi
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Fibronectin Binding

Adherence and fibronectin binding are environmentally regulated in the group A streptococci

1993 ◽  
Vol 9 (6) ◽  
pp. 1213-1222 ◽  
Author(s):  
Tambryn VanHeyningen ◽  
George Fogg ◽  
Debra Yates ◽  
Emanuel Hanski ◽  
Michael Caparon
Keyword(s):  
Group A Streptococci ◽  
Group A ◽  
Fibronectin Binding

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 Protective Immunity againstStreptococcus pyogenesChallenge in Mice after Immunization with Fibronectin‐Binding Protein

2005 ◽  
Vol 192 (12) ◽  
pp. 2081-2091 ◽  
Author(s):  
Yutaka Terao ◽  
Shigefumi Okamoto ◽  
Kosuke Kataoka ◽  
Shigeyuki Hamada ◽  
Shigetada Kawabata
Keyword(s):  
Protective Immunity ◽  
Binding Protein ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

scholarly journals Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs

PLoS ONE ◽  
2016 ◽  
Vol 11 (7) ◽  
pp. e0159118 ◽  
Author(s):  
Xiaowen Liang ◽  
Brandon L. Garcia ◽  
Livia Visai ◽  
Sabitha Prabhakaran ◽  
Nicola A. G. Meenan ◽  
...  
Keyword(s):  
Allosteric Regulation ◽  
Fibronectin Binding
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