Journal
JOURNAL OF MOLECULAR RECOGNITION
Volume 21, Issue 4, Pages 210-216Publisher
WILEY
DOI: 10.1002/jmr.886
Keywords
molecular force spectroscopy; atomic force microscopy (AFM); junctional adhesion molecule-A (JAM-A); reovirus attachment protein (sigma1)
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Funding
- NCI NIH HHS [P30 CA068485, CA68485] Funding Source: Medline
- NIDDK NIH HHS [P30 DK020593, DK20593] Funding Source: Medline
- NIGMS NIH HHS [T32 GM08554, T32 GM008554, R01 GM67853, R01 GM067853] Funding Source: Medline
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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, sigma 1. In this study, we used single molecular force spectroscopy to compare the kinetics of JAM-A interactions with itself and sigma 1. A chimeric murine JAM-A/Fc fusion protein and the purified sigma 1 head domain were used to probe murine L929 cells, which express JAM-A and are susceptible to reovirus infection. The bond half-life [t(1/2)) of homophilic JAM-A interactions was found to be shorter (k(off)(o) = 0.688 +/- 0.349 s(-1)) than that of sigma 1/JAM-A interactions (k(off)(o) = 0.067 +/- 0.041 s-1). These results are in accordance with the physiological of functions of JAM-A and sigma 1. A short bond lifetime imparts a highly dynamic nature to homophilic JAM-A interactions for regulating tight junction permeability while stable interactions between sigma 1 and JAM-A likely anchor the virus to the cell surface and facilitate viral entry. Copyright (C) 2008 John Wiley & Sons, Ltd.
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