Document Detail


Glycoprotein E of varicella-zoster virus enhances cell-cell contact in polarized epithelial cells.
MedLine Citation:
PMID:  11070038     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Varicella-zoster virus (VZV) infection involves the cell-cell spread of virions, but how viral proteins interact with the host cell membranes that comprise intercellular junctions is not known. Madin-Darby canine kidney (MDCK) cells were constructed to express the glycoproteins gE, gI, or gE/gI constitutively and were used to examine the effects of these VZV glycoproteins in polarized epithelial cells. At low cell density, VZV gE induced partial tight junction (TJ) formation under low-calcium conditions, whether expressed alone or with gI. Although most VZV gE was intracellular, gE was also shown to colocalize with the TJ protein ZO-1 with or without concomitant expression of gI. Freeze fracture electron microscopy revealed normal TJ strand morphology in gE-expressing MDCK cells. Functionally, the expression of gE was associated with a marked acceleration in the establishment of maximum transepithelial electrical resistance (TER) in MDCK-gE cells; MDCK-gI and MDCK-gE/gI cells exhibited a similar pattern of early TER compared to MDCK cells, although peak resistances were lower than those of gE alone. VZV gE expression altered F-actin organization and lipid distribution, but coexpression of gI modulated these effects. Two regions of the gE ectodomain, amino acids (aa) 278 to 355 and aa 467 to 498, although lacking Ca(2+) binding motifs, exhibit similarities with corresponding regions of the cell adhesion molecules, E-cadherin and desmocollin. These observations suggest that VZV gE and gE/gI may contribute to viral pathogenesis by facilitating epithelial cell-cell contacts.
Authors:
C Mo; E E Schneeberger; A M Arvin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of virology     Volume:  74     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  2000 Dec 
Date Detail:
Created Date:  2000-12-04     Completed Date:  2000-12-04     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  11377-87     Citation Subset:  IM    
Affiliation:
Department of Pediatrics, Stanford University School of Medicine, Stanford, California 94305, USA. cmo@cmgm.stanford.edu
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MeSH Terms
Descriptor/Qualifier:
Actins / analysis
Amino Acid Sequence
Animals
Cadherins / chemistry
Cell Communication*
Cell Line
Cell Polarity
Cytoskeletal Proteins / chemistry
Desmocollins
Desmoplakins
Dogs
Electric Impedance
Epithelial Cells / physiology
Herpesvirus 3, Human / physiology*
Lipids / analysis
Molecular Sequence Data
Sequence Homology, Amino Acid
Tight Junctions
Viral Envelope Proteins / physiology*
Grant Support
ID/Acronym/Agency:
AI20459/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Actins; 0/Cadherins; 0/Cytoskeletal Proteins; 0/Desmocollins; 0/Desmoplakins; 0/Lipids; 0/Viral Envelope Proteins; 0/glycoprotein gp1, varicella-zoster virus
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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