A Simple Theory for Molecular Chemotaxis Driven by Specific Binding Interactions

Author(s):  
Kathleen T. Krist ◽  
Ayusman Sen ◽  
Will G Noid
2009 ◽  
Vol 75 (7) ◽  
pp. 2236-2237 ◽  
Author(s):  
Janete A. D. Sena ◽  
Carmen Sara Hernández-Rodríguez ◽  
Juan Ferré

ABSTRACT Vip3Aa, Vip3Af, Cry1Ab, and Cry1Fa were tested for their toxicities and binding interactions. Vip3A proteins were more toxic than Cry1 proteins. Binding assays showed independent specific binding sites for Cry1 and Vip3A proteins. Cry1Ab and Cry1Fa competed for the same binding sites, whereas Vip3Aa competed for those of Vip3Af.


2003 ◽  
Vol 69 (8) ◽  
pp. 4474-4481 ◽  
Author(s):  
Andrea Hanna ◽  
Michael Berg ◽  
Valerie Stout ◽  
Anneta Razatos

ABSTRACT Urinary tract infections are the most common urologic disease in the United States and one of the most common bacterial infections of any organ system. Biofilms persist in the urinary tract and on catheter surfaces because biofilm microorganisms are resistant to host defense mechanisms and antibiotic therapy. The first step in the establishment of biofilm infections is bacterial adhesion; preventing bacterial adhesion represents a promising method of controlling biofilms. Evidence suggests that capsular polysaccharides play a role in adhesion and pathogenicity. This study focuses on the role of physiochemical and specific binding interactions during adhesion of colanic acid exopolysaccharide mutant strains. Bacterial adhesion was evaluated for isogenic uropathogenic Escherichia coli strains that differed in colanic acid expression. The atomic force microscope (AFM) was used to directly measure the reversible physiochemical and specific binding interactions between bacterial strains and various substrates as bacteria initially approach the interface. AFM results indicate that electrostatic interactions were not solely responsible for the repulsive forces between the colanic acid mutant strains and hydrophilic substrates. Moreover, hydrophobic interactions were not found to play a significant role in adhesion of the colanic acid mutant strains. Adhesion was also evaluated by parallel-plate flow cell studies in comparison to AFM force measurements to demonstrate that prolonged incubation times alter bacterial adhesion. Results from this study demonstrate that the capsular polysaccharide colanic acid does not enhance bacterial adhesion but rather blocks the establishment of specific binding as well as time-dependent interactions between uropathogenic E. coli and inert substrates.


1994 ◽  
Vol 22 (2) ◽  
pp. 213S-213S
Author(s):  
GEOFFREY W. MELLOR ◽  
MARK P. THOMAS ◽  
SHERAZ GUL ◽  
MICHAEL A. NOBLE ◽  
EMRYS W. THOMAS ◽  
...  

2021 ◽  
Vol 9 ◽  
Author(s):  
Andreas Erichsen ◽  
Dennis Larsen ◽  
Sophie R. Beeren

We demonstrate how different anions from across the Hofmeister series can influence the behavior of enzyme-mediated dynamic combinatorial libraries of cyclodextrins (CDs). Using cyclodextrin glucanotransferase to catalyze reversible transglycosylation, dynamic mixtures of interconverting cyclodextrins can be formed wherein the relative concentrations of α-CD, β-CD and γ-CD is determined by their intrinsic stabilities and any stabilizing influences of added template (guest) molecules. Here, we find that addition of high concentrations of kosmotropic anions can be used to enhance the effects of added hydrophobic templates, while chaotropic anions can themselves act as templates, causing predictable and significant changes in the cyclodextrin composition due to weak, but specific, binding interactions with α-CD.


1992 ◽  
Vol 10 (3) ◽  
pp. 565-575 ◽  
Author(s):  
F. Adnet ◽  
J. Liquier ◽  
E. Taillandier ◽  
Malvinder P. Singh ◽  
K. Ekambareswara Rao ◽  
...  

2015 ◽  
Vol 26 (7) ◽  
pp. 1371-1385 ◽  
Author(s):  
Mary Katherine Bradford ◽  
Karen Whitworth ◽  
Beverly Wendland

Endocytosis is a well-conserved process by which cells invaginate small portions of the plasma membrane to create vesicles containing extracellular and transmembrane cargo proteins. Dozens of proteins and hundreds of specific binding interactions are needed to coordinate and regulate these events. Saccharomyces cerevisiae is a powerful model system with which to study clathrin-mediated endocytosis (CME). Pan1 is believed to be a scaffolding protein due to its interactions with numerous proteins that act throughout the endocytic process. Previous research characterized many Pan1 binding interactions, but due to Pan1's essential nature, the exact mechanisms of Pan1's function in endocytosis have been difficult to define. We created a novel Pan1-degron allele, Pan1-AID, in which Pan1 can be specifically and efficiently degraded in <1 h upon addition of the plant hormone auxin. The loss of Pan1 caused a delay in endocytic progression and weakened connections between the coat/actin machinery and the membrane, leading to arrest in CME. In addition, we determined a critical role for the central region of Pan1 in endocytosis and viability. The regions important for endocytosis and viability can be separated, suggesting that Pan1 may have a distinct role in the cell that is essential for viability.


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