scholarly journals A possible role of cellulose-binding protein A (CBPA) in the adhesion of Eubacterium cellulosolvens 5 to cellulose

2003 ◽  
Vol 49 (4) ◽  
pp. 245-250 ◽  
Author(s):  
Atsushi Toyoda ◽  
Kazunori Takano ◽  
Hajime Minato
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Eubacterium Cellulosolvens ◽  
Cellulose Binding

scholarly journals Assessment of the Dual Role of Clumping Factor A in S. Aureus Adhesion to Endothelium in Absence and Presence of Plasma

2018 ◽  
Vol 118 (07) ◽  
pp. 1230-1241 ◽  
Author(s):  
Jorien Claes ◽  
Bartosz Ditkowski ◽  
Laurens Liesenborghs ◽  
Tiago Veloso ◽  
Jose Entenza ◽  
...  
Keyword(s):  
Infective Endocarditis ◽  
Binding Protein ◽  
Protein A ◽  
Bacterial Proteins ◽  
Fibronectin Binding Protein ◽  
A Disintegrin And Metalloproteinase ◽  
Von Willebrand ◽  
Willebrand Factor

AbstractAdhesion of Staphylococcus aureus to endothelial cells (ECs) is paramount in infective endocarditis. Bacterial proteins such as clumping factor A (ClfA) and fibronectin binding protein A (FnbpA) mediate adhesion to EC surface molecules and (sub)endothelial matrix proteins including fibrinogen (Fg), fibrin, fibronectin (Fn) and von Willebrand factor (vWF). We studied the influence of shear flow and plasma on the binding of ClfA and FnbpA (including its sub-domains A, A16+, ABC, CD) to coverslip-coated vWF, Fg/fibrin, Fn or confluent ECs, making use of Lactococcus lactis, expressing these adhesins heterologously. Global adherence profiles were similar in static and flow conditions. In the absence of plasma, L. lactis-clfA binding to Fg increased with shear forces, whereas binding to fibrin did not. The degree of adhesion of L. lactis-fnbpA to EC-bound Fn and of L. lactis-clfA to EC-bound Fg, furthermore, was similar to that of L. lactis-clfA to coated vWF domain A1, in the presence of vWF-binding protein (vWbp). Yet, in plasma, L. lactis-clfA adherence to activated EC-vWF/vWbp dropped over 10 minutes by 80% due to vWF-hydrolysis by a disintegrin and metalloproteinase with thrombospondin type 1 motif, member 13 and that of L. lactis-fnbpA likewise by > 70% compared to the adhesion in absence of plasma. In contrast, plasma Fg supported high L. lactis-clfA binding to resting and activated ECs. Or, in plasma S. aureus adhesion to active endothelium occurs mainly via two complementary pathways: a rapid but short-lived vWF/vWbp pathway and a stable integrin-coupled Fg-pathway. Hence, the pharmacological inhibition of ClfA-Fg interactions may constitute a valuable additive treatment in infective endocarditis.

scholarly journals FANCJ (BACH1) helicase forms DNA damage inducible foci with replication protein A and interacts physically and functionally with the single-stranded DNA-binding protein

Blood ◽  
2007 ◽  
Vol 110 (7) ◽  
pp. 2390-2398 ◽  
Author(s):  
Rigu Gupta ◽  
Sudha Sharma ◽  
Joshua A. Sommers ◽  
Mark K. Kenny ◽  
Sharon B. Cantor ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Binding ◽  
Binding Protein ◽  
Critical Role ◽  
Protein A ◽  
Replication Protein A ◽  
Dna Binding Protein ◽  
Replication Protein ◽  
Single Stranded Dna

The BRCA1 associated C-terminal helicase (BACH1, designated FANCJ) is implicated in the chromosomal instability genetic disorder Fanconi anemia (FA) and hereditary breast cancer. A critical role of FANCJ helicase may be to restart replication as a component of downstream events that occur during the repair of DNA cross-links or double-strand breaks. We investigated the potential interaction of FANCJ with replication protein A (RPA), a single-stranded DNA-binding protein implicated in both DNA replication and repair. FANCJ and RPA were shown to coimmunoprecipitate most likely through a direct interaction of FANCJ and the RPA70 subunit. Moreover, dependent on the presence of BRCA1, FANCJ colocalizes with RPA in nuclear foci after DNA damage. Our data are consistent with a model in which FANCJ associates with RPA in a DNA damage-inducible manner and through the protein interaction RPA stimulates FANCJ helicase to better unwind duplex DNA substrates. These findings identify RPA as the first regulatory partner of FANCJ. The FANCJ-RPA interaction is likely to be important for the role of the helicase to more efficiently unwind DNA repair intermediates to maintain genomic stability.

scholarly journals Role of conserved residues in structure and stability: Tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily

2009 ◽  
Vol 10 (11) ◽  
pp. 2301-2316 ◽  
Author(s):  
Lesley H. Greene ◽  
Evangelia D. Chrysina ◽  
Laurence I. Irons ◽  
Anastassios C. Papageorgiou ◽  
K. Ravi Acharya ◽  
...  
Keyword(s):  
Human Serum ◽  
Binding Protein ◽  
Protein A ◽  
Retinol Binding Protein ◽  
Serum Retinol ◽  
Conserved Residues ◽  
Structure And Stability

scholarly journals Characterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A.

1993 ◽  
Vol 175 (18) ◽  
pp. 5762-5768 ◽  
Author(s):  
M A Goldstein ◽  
M Takagi ◽  
S Hashida ◽  
O Shoseyov ◽  
R H Doi ◽  
...  
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Clostridium Cellulovorans ◽  
Cellulose Binding

scholarly journals Coactosin-like protein, a human F-actin-binding protein: critical role of lysine-75

2001 ◽  
Vol 359 (2) ◽  
pp. 255 ◽  
Author(s):  
Patrick PROVOST ◽  
Johanne DOUCET ◽  
Alexander STOCK ◽  
Günther GERISCH ◽  
Bengt SAMUELSSON ◽  
...  
Keyword(s):  
Binding Protein ◽  
Critical Role ◽  
Protein A ◽  
Actin Binding ◽  
Actin Binding Protein

scholarly journals Role of fibronectin-binding protein A in Clostridium difficile intestinal colonization

2011 ◽  
Vol 60 (8) ◽  
pp. 1155-1161 ◽  
Author(s):  
Amira Barketi-Klai ◽  
Sandra Hoys ◽  
Sylvie Lambert-Bordes ◽  
Anne Collignon ◽  
Imad Kansau
Keyword(s):  
Clostridium Difficile ◽  
Binding Protein ◽  
Protein A ◽  
Intestinal Colonization ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding
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