The Two-Pathway Model of the Biological Catch-Bond as a Limit of the Allosteric Model

Pereverzev, Yuriy V.; Prezhdo, Eugenia; Sokurenko, Evgeni V.

doi:10.1016/j.bpj.2011.09.005

Cited by 24 publications

(19 citation statements)

References 51 publications

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“…They are dubbed catch bonds and are thought to characterize TCR interactions involving pMHC agonists (56). Note that despite a number of studies, the structural mechanisms that underlie catch bond behavior, including those postulated for the TCR, remain poorly understood (57)(58)(59). Second, bond formation is a multistep process leading to a progressive increase in bond stability.…”

Section: Tcr Mechanosensing As the Initiating Eventmentioning

confidence: 98%

Early T Cell Activation: Integrating Biochemical, Structural, and Biophysical Cues

Malissen

Bongrand

2015

Annu. Rev. Immunol.

120

114

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T cells carry out the formidable task of identifying small numbers of foreign antigenic peptides rapidly and specifically against a very noisy environmental background of endogenous self-peptides. Early steps in T cell activation have thus fascinated biologists and are among the best-studied models of cell stimulation. This remarkable process, critical in adaptive immune responses, approaches and even seems to exceed the limitations set by the physical laws ruling molecular behavior. Despite the enormous amount of information concerning the nature of molecules involved in the T cell antigen receptor (TCR) signal transduction network, and the description of the nanoscale organization and real-time analysis of T cell responses, the general principles of information gathering and processing remain incompletely understood. Here we review currently accepted key data on TCR function, discuss the limitations of current research strategies, and suggest a novel model of TCR triggering and a few promising ways of going further into the integration of available data.

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Section: Tcr Mechanosensing As the Initiating Eventmentioning

confidence: 98%

Early T Cell Activation: Integrating Biochemical, Structural, and Biophysical Cues

Malissen

Bongrand

2015

Annu. Rev. Immunol.

120

114

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“…Correspondingly, a one state two path approach is not applicable to our experimental data as it diverges in the low force regime. More elaborate approaches have been reported that take account of force-induced deformations (29), protein water interfaces (50), fluctuating energy barriers (26), or two bound states separated by an energy barrier (22,23,28,(31)(32)(33)48).…”

Section: Single Molecule Force Clamp Experimentsconstant Force Experimentioning

confidence: 99%

“…Namely, catch bond behavior could be found in PSel-PSGL-1 (4), FimH-mannose (18), actomyosin (19), platelet glycoprotein Iba-von Willebrand factor (20), and integrins (21) thus verifying the general concept of this most exciting and paradox discovery in cell adhesion. Beyond its experimental findings a couple of theoretical models were formulated helping to rationalize this counterintuitive phenomenon (22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33).…”

Section: Introductionmentioning

confidence: 99%

Catch Bond Interaction between Cell-Surface Sulfatase Sulf1 and Glycosaminoglycans

Harder

Möller

Milz

et al. 2015

Biophysical Journal

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In biological adhesion, the biophysical mechanism of specific biomolecular interaction can be divided in slip and catch bonds, respectively. Conceptually, slip bonds exhibit a reduced bond lifetime under increased external force and catch bonds, in contrast, exhibit an increased lifetime (for a certain force interval). Since 2003, a handful of biological systems have been identified to display catch bond properties. Upon investigating the specific interaction between the unique hydrophilic domain (HD) of the human cell-surface sulfatase Sulf1 against its physiological glycosaminoglycan (GAG) target heparan sulfate (HS) by single molecule force spectroscopy (SMFS), we found clear evidence of catch bond behavior in this system. The HD, ∼320 amino acids long with dominant positive charge, and its interaction with sulfated GAG-polymers were quantitatively investigated using atomic force microscopy (AFM) based force clamp spectroscopy (FCS) and dynamic force spectroscopy (DFS). In FCS experiments, we found that the catch bond character of HD against GAGs could be attributed to the GAG 6-O-sulfation site whereas only slip bond interaction can be observed in a GAG system where this site is explicitly lacking. We interpreted the binding data within the theoretical framework of a two state two path model, where two slip bonds are coupled forming a double-well interaction potential with an energy difference of ΔE ≈ 9 kBT and a compliance length of Δx ≈ 3.2 nm. Additional DFS experiments support this assumption and allow identification of these two coupled slip-bond states that behave consistently within the Kramers-Bell-Evans model of force-mediated dissociation.

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“…83 This type of surface is relevant for modeling the so-called catch bonds. [84][85][86][87][88][89][90][91][92][93][94][95][96][97]…”

Section: Potential Energy Surface With An Elementary Pathwaymentioning

confidence: 99%

Analysis of the Acting Forces in a Theory of Catalysis and Mechanochemistry

Quapp

Bofill²,

Ribas‐Ariño³

2017

J. Phys. Chem. A

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The theoretical description of a chemical process resulting from the application of mechanical or catalytical stress to a molecule is performed by the generation of an effective potential energy surface (PES). Changes for minima and saddle points by the stress are described by Newton trajectories (NTs) on the original PES. From the analysis of the acting forces we postulate the existence of pulling corridors built by families of NTs that connect the same stationary points. For different exit saddles of different height we discuss the corresponding pulling corridors; mainly by simple two-dimensional surface models. If there are different exit saddles then there can exist saddles of index two, at least, between. Then the case that a full pulling corridor crosses a saddle of index two is the normal case. It leads to an intrinsic hysteresis of such pullings for the forward or the backward reaction. Assuming such relations we can explain some results in the literature. A new finding is the existence of roundabout corridors that can switch between different saddle points by a reversion of the direction. The findings concern the mechanochemistry of molecular systems under a mechanical load as well as the electrostatic force and can be extended to catalytic and enzymatic accelerated reactions. The basic and ground ansatz includes both kinds of forces in a natural way without an extra modification.

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The Two-Pathway Model of the Biological Catch-Bond as a Limit of the Allosteric Model

Cited by 24 publications

References 51 publications

Early T Cell Activation: Integrating Biochemical, Structural, and Biophysical Cues

Early T Cell Activation: Integrating Biochemical, Structural, and Biophysical Cues

Catch Bond Interaction between Cell-Surface Sulfatase Sulf1 and Glycosaminoglycans

Analysis of the Acting Forces in a Theory of Catalysis and Mechanochemistry

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