CAR modulates E-cadherin dynamics in the presence of adenovirus type 5

Adenovirus (Ad) serotype 5 (Ad5) fiber competitively binds to the coxsackievirus and Ad receptor (CAR) to attach Ad5 to target cells and also disrupts cell junctions and facilitates virus escape at a late stage in Ad5 infection. Here we demonstrate that paracellular permeability in MCF7 and CAR over...

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Bibliographic Details
Published in:PloS one 2011-08, Vol.6 (8), p.e23056-e23056
Main Authors: Hussain, Fawziyah, Morton, Penny E, Snippe, Marjolein, Sullivan, Janis, Farmer, Charlotte, Martin-Fernandez, Marisa L, Parsons, Maddy, Santis, George
Format: Article
Language:English
Subjects:
Adenoviridae - metabolism
Adenovirus
Adenoviruses
Asthma
beta Catenin - genetics
beta Catenin - metabolism
Biology
Blotting, Western
Cadherins - genetics
Cadherins - metabolism
Cell adhesion
Cell adhesion & migration
Cell Adhesion - genetics
Cell Adhesion - physiology
Cell Division - genetics
Cell Division - physiology
Cell junctions
Cell Line, Tumor
Coxsackie and Adenovirus Receptor-Like Membrane Protein
Coxsackievirus
Coxsackievirus infections
E-cadherin
Fluorescence Recovery After Photobleaching
Health aspects
Humans
Immunoprecipitation
Infections
Intercellular Junctions - genetics
Intercellular Junctions - metabolism
Kinases
Localization
Lung cancer
Microscopy, Confocal
Molecular dynamics
Permeability
Protein Binding
Proteins
Receptors
Receptors, Virus - genetics
Receptors, Virus - metabolism
Recovery (Medical)
Viruses
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Description
Summary:Adenovirus (Ad) serotype 5 (Ad5) fiber competitively binds to the coxsackievirus and Ad receptor (CAR) to attach Ad5 to target cells and also disrupts cell junctions and facilitates virus escape at a late stage in Ad5 infection. Here we demonstrate that paracellular permeability in MCF7 and CAR overexpressing MCF7 (FLCARMCF7) cells is increased within minutes following the addition of Ad5 to cells. This is brought about, at least in part, by altering the molecular dynamics of E-cadherin, a key component of the cell-cell adhesion complex. We also demonstrate that the increase in E-cadherin mobility is constitutively altered by the presence of CAR at FLCARMCF7 cell junctions. As increased paracellular permeability was observed early after the addition of Ad5 to cells, we postulate that this may represent a mechanism by which Ad5 could disrupt cell junctions to facilitate further access to its cell receptors.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0023056