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- Title
A comparative molecular force spectroscopy study of homophilic JAM-A interactions and JAM-A interactions with reovirus attachment protein σ1.
- Authors
Vedula, Sri Ram Krishna; Lim, Tong Seng; Kirchner, Eva; Guglielmi, Kristen M.; Dermody, Terence S.; Stehle, Thilo; Hunziker, Walter; Lim, Chwee Teck
- Abstract
JAM-A belongs to a family of immunoglobulin-like proteins called junctional adhesion molecules (JAMs) that localize at epithelial and endothelial intercellular tight junctions. JAM-A is also expressed on dendritic cells, neutrophils, and platelets. Homophilic JAM-A interactions play an important role in regulating paracellular permeability and leukocyte transmigration across epithelial monolayers and endothelial cell junctions, respectively. In addition, JAM-A is a receptor for the reovirus attachment protein, σ1. In this study, we used single molecular force spectroscopy to compare the kinetics of JAM-A interactions with itself and σ1. A chimeric murine JAM-A/Fc fusion protein and the purified σ1 head domain were used to probe murine L929 cells, which express JAM-A and are susceptible to reovirus infection. The bond half-life ( t1/2) of homophilic JAM-A interactions was found to be shorter ( $k_{{\bf off}}^{\bf o} = 0.688 \pm 0.349\;{\bf s}^{ - 1} $) than that of σ1/JAM-A interactions ( $k_{{\bf off}}^{\bf o} = 0.067 \pm 0.041\;{\bf s}^{ - 1} $). These results are in accordance with the physiological functions of JAM-A and σ1. A short bond lifetime imparts a highly dynamic nature to homophilic JAM-A interactions for regulating tight junction permeability while stable interactions between σ1 and JAM-A likely anchor the virus to the cell surface and facilitate viral entry. Copyright © 2008 John Wiley & Sons, Ltd.
- Publication
Journal of Molecular Recognition, 2008, Vol 21, Issue 4, p210
- ISSN
0952-3499
- Publication type
Article
- DOI
10.1002/jmr.886