Faculty Opinions recommendation of Catch bonds govern adhesion through L-selectin at threshold shear.

Biological adhesion is frequently mediated by specific membrane proteins (adhesion molecules). Starting with the notion of adhesion molecules, we present a simple model of the physics of membrane-to-surface attachment and detachment. This model consists of coupling the equations for deformation of an elastic membrane with equations for the chemical kinetics of the adhesion molecules. We propose a set of constitutive laws relating bond stress to bond strain and also relating the chemical rate constants of the adhesion molecules to bond strain. We derive an exact formula for the critical tension. We also describe a fast and accurate finite difference algorithm for generating numerical solutions of our model. Using this algorithm, we are able to compute the transient behaviour during the initial phases of adhesion and detachment as well as the steady-state geometry of adhesion and the velocity of the contact. An unexpected consequence of our model is the predicted occurrence of states in which adhesion cannot be reversed by application of tension. Such states occur only if the adhesion molecules have certain constitutive properties (catch-bonds). We discuss the rational for such catch-bonds and their possible biological significance. Finally, by analysis of numerical solutions, we derive an accurate and general expression for the steady-state velocity of attachment and detachment. As applications of the theory, we discuss data on the rolling velocity of granulocytes in post-capillary venules and data on lectin-mediated adhesion of red cells.

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For catch bonds, it all hinges on the interdomain region

The Journal of Cell Biology ◽

10.1083/jcb.200609029 ◽

2006 ◽

Vol 174 (7) ◽

pp. 911-913 ◽

Cited By ~ 18

Author(s):

Wendy Thomas

Keyword(s):

Sialyl Lewis X ◽

Adhesive Bonds ◽

Structural Mechanism ◽

Adhesive Protein ◽

Sialyl Lewis ◽

Biological Adhesive ◽

Actin Motor ◽

Selectin Binding ◽

Cell Adhesion Proteins ◽

Catch Bonds

Tensile mechanical force was long assumed to increase the detachment rates of biological adhesive bonds (Bell, 1978). However, in the last few years, several receptor–ligand pairs were shown to form “catch bonds,” whose lifetimes are enhanced by moderate amounts of force. These include the bacterial adhesive protein FimH binding to its ligand mannose (Thomas et al., 2002; Thomas et al., 2006), blood cell adhesion proteins P- and L-selectin binding to sialyl Lewis X (sLeX)–containing ligands (Marshall et al., 2003; Evans et al., 2004; Sarangapani et al., 2004), and the myosin–actin motor protein interaction (Guo and Guilford, 2006). The structural mechanism behind this counterintuitive force–enhanced catch bond behavior is of great interest.

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Force-Dependent Facilitated Dissociation Can Generate Protein-DNA Catch Bonds

Biophysical Journal ◽

10.1016/j.bpj.2019.07.044 ◽

2019 ◽

Vol 117 (6) ◽

pp. 1085-1100

Author(s):

Katelyn Dahlke ◽

Jing Zhao ◽

Charles E. Sing ◽

Edward J. Banigan

Keyword(s):

Catch Bonds

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Principles for enhancing virus capsid capacity and stability from a thermophilic virus capsid structure

Nature Communications ◽

10.1038/s41467-019-12341-z ◽

2019 ◽

Vol 10 (1) ◽

Cited By ~ 6

Author(s):

Nicholas P. Stone ◽

Gabriel Demo ◽

Emily Agnello ◽

Brian A. Kelch

Keyword(s):

Major Capsid Protein ◽

Extreme Environment ◽

Structural Basis ◽

Genome Packaging ◽

Virus Capsid ◽

Dna Viruses ◽

Double Stranded Dna ◽

High Internal Pressure ◽

Extracellular Environment ◽

Catch Bonds

Abstract The capsids of double-stranded DNA viruses protect the viral genome from the harsh extracellular environment, while maintaining stability against the high internal pressure of packaged DNA. To elucidate how capsids maintain stability in an extreme environment, we use cryoelectron microscopy to determine the capsid structure of thermostable phage P74-26 to 2.8-Å resolution. We find P74-26 capsids exhibit an overall architecture very similar to those of other tailed bacteriophages, allowing us to directly compare structures to derive the structural basis for enhanced stability. Our structure reveals lasso-like interactions that appear to function like catch bonds. This architecture allows the capsid to expand during genome packaging, yet maintain structural stability. The P74-26 capsid has T = 7 geometry despite being twice as large as mesophilic homologs. Capsid capacity is increased with a larger, flatter major capsid protein. Given these results, we predict decreased icosahedral complexity (i.e. T ≤ 7) leads to a more stable capsid assembly.

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Effect of loading conditions on the dissociation behaviour of catch bond clusters

Journal of The Royal Society Interface ◽

10.1098/rsif.2011.0553 ◽

2011 ◽

Vol 9 (70) ◽

pp. 928-937 ◽

Cited By ~ 19

Author(s):

L. Sun ◽

Q. H. Cheng ◽

H. J. Gao ◽

Y. W. Zhang

Keyword(s):

Multiple Bond ◽

Tensile Load ◽

Load Sharing ◽

Loading Conditions ◽

Bond Behaviour ◽

Catch Bond ◽

Linear Load ◽

Bond System ◽

Bond Mechanism ◽

Catch Bonds

Under increasing tensile load, the lifetime of a single catch bond counterintuitively increases up to a maximum and then decreases exponentially like a slip bond. So far, the characteristics of single catch bond dissociation have been extensively studied. However, it remains unclear how a cluster of catch bonds behaves under tensile load. We perform computational analysis on the following models to examine the characteristics of clustered catch bonds: (i) clusters of catch bonds with equal load sharing, (ii) clusters of catch bonds with linear load sharing, and (iii) clusters of catch bonds in micropipette-manipulated cell detachment. We focus on the differences between the slip and catch bond clusters, identifying the critical factors for exhibiting the characteristics of catch bond mechanism for the multiple-bond system. Our computation reveals that for a multiple-bond cluster, the catch bond behaviour could only manifest itself under relatively uniform loading conditions and at certain stages of decohesion, explaining the difficulties in observing the catch bond mechanism under real biological conditions.

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