scholarly journals Structural Insights into the Ligand Binding and Releasing Mechanism of Antheraea polyphemus Pheromone-Binding Protein 1: Role of the C-Terminal Tail

Biochemistry ◽  
2013 ◽  
Vol 52 (6) ◽  
pp. 1037-1044 ◽  
Author(s):  
Uma V. Katre ◽  
Suman Mazumder ◽  
Smita Mohanty
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Antheraea Polyphemus ◽  
Pheromone Binding Protein ◽  
Structural Insights

scholarly journals The Crystal Structure of a Cockroach Pheromone-binding Protein Suggests a New Ligand Binding and Release Mechanism

2003 ◽  
Vol 278 (32) ◽  
pp. 30213-30218 ◽  
Author(s):  
Audrey Lartigue ◽  
Arnaud Gruez ◽  
Silvia Spinelli ◽  
Stéphane Rivière ◽  
Rémy Brossut ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Binding Protein ◽  
Release Mechanism ◽  
Pheromone Binding Protein

The interrelationship between ligand binding and self-association of the folate binding protein. The role of detergent–tryptophan interaction

2011 ◽  
Vol 1810 (12) ◽  
pp. 1330-1339 ◽  
Author(s):  
Jan Holm ◽  
Christian Schou ◽  
Linnea N. Babol ◽  
Anders J. Lawaetz ◽  
Susanne W. Bruun ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Folate Binding Protein ◽  
Self Association

scholarly journals Mechanical Strength and Inhibition of theStaphylococcus aureusCollagen-Binding Protein Cna

mBio ◽  
2016 ◽  
Vol 7 (5) ◽  
Author(s):  
Philippe Herman-Bausier ◽  
Claire Valotteau ◽  
Giampiero Pietrocola ◽  
Simonetta Rindi ◽  
David Alsteens ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Monoclonal Antibodies ◽  
Ligand Binding ◽  
Mechanical Strength ◽  
Mechanical Response ◽  
Binding Protein ◽  
Adhesion Proteins ◽  
High Affinity ◽  
Living Bacteria

ABSTRACTThe bacterial pathogenStaphylococcus aureusexpresses a variety of cell surface adhesion proteins that bind to host extracellular matrix proteins. Among these, the collagen (Cn)-binding protein Cna plays important roles in bacterium-host adherence and in immune evasion. While it is well established that the A region of Cna mediates ligand binding, whether the repetitive B region has a dedicated function is not known. Here, we report the direct measurement of the mechanical strength of Cna-Cn bonds on living bacteria, and we quantify the antiadhesion activity of monoclonal antibodies (MAbs) targeting this interaction. We demonstrate that the strength of Cna-Cn bondsin vivois very strong (~1.2 nN), consistent with the high-affinity “collagen hug” mechanism. The B region is required for strong ligand binding and has been found to function as a spring capable of sustaining high forces. This previously undescribed mechanical response of the B region is of biological significance as it provides a means to project the A region away from the bacterial surface and to maintain bacterial adhesion under conditions of high forces. We further quantified the antiadhesion activity of MAbs raised against the A region of Cna directly on living bacteria without the need for labeling or purification. Some MAbs are more efficient in blocking single-cell adhesion, suggesting that they act as competitive inhibitors that bind Cna residues directly involved in ligand binding. This report highlights the role of protein mechanics in activating the function of staphylococcal adhesion proteins and emphasizes the potential of antibodies to prevent staphylococcal adhesion and biofilm formation.IMPORTANCECna is a collagen (Cn)-binding protein fromStaphylococcus aureusthat is involved in pathogenesis. Currently, we know little about the functional role of the repetitive B region of the protein. Here, we unravel the mechanical strength of Cna in living bacteria. We show that single Cna-Cn bonds are very strong, reflecting high-affinity binding by the collagen hug mechanism. We discovered that the B region behaves as a nanospring capable of sustaining high forces. This unanticipated mechanical response, not previously described for any staphylococcal adhesin, favors a model in which the B region has a mechanical function that is essential for strong ligand binding. Finally, we assess the antiadhesion activity of monoclonal antibodies against Cna, suggesting that they could be used to inhibitS. aureusadhesion.

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