Document Detail


Regulation of varicella-zoster virus-induced cell-to-cell fusion by the endocytosis-competent glycoproteins gH and gE.
MedLine Citation:
PMID:  14990707     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The gH glycoprotein of varicella-zoster virus (VZV) is a major fusogen. The realigned short cytoplasmic tail of gH (18 amino acids) harbors a functional endocytosis motif (YNKI) that mediates internalization in both VZV-infected and transfected cells (T. J. Pasieka, L. Maresova, and C. Grose, J. Virol. 77: 4194-4202, 2003). During subsequent confocal microscopy studies of endocytosis-deficient gH mutants, we observed that cells transfected with the gH tail mutants exhibited marked fusion. Therefore, we postulated that VZV gH endocytosis served to regulate cell-to-cell fusion. Subsequent analyses of gH+gL transfection fusion assays by the Kolmogorov-Smirnov statistical test demonstrated that expression of the endocytosis-deficient gH mutants resulted in a statistically significant enhancement of cell-to-cell fusion (P < 0.0001) compared to wild-type gH. On the other hand, coexpression of VZV gE, another endocytosis-competent VZV glycoprotein, was able to temper the fusogenicity of the gH endocytosis mutants by facilitating internalization of the mutant gH protein from the cell surface. When the latter results were similarly analyzed, there was no longer any enhanced fusion by the endocytosis-deficient gH mutant protein. In summary, these studies support a role for gH endocytosis in regulating the cell surface expression of gH and thereby regulating gH-mediated fusion. The data also confirm and extend prior observations of a gE-gH interaction during viral glycoprotein trafficking in a VZV transfection system.
Authors:
Tracy Jo Pasieka; Lucie Maresova; Kimiyasu Shiraki; Charles Grose
Related Documents :
4340167 - Effect of environmental ph on the efficiency of cellular hybridization.
15232107 - Lack of a fusion requirement for development of bone marrow-derived epithelia.
2040567 - Ultrastructural changes of the midgut epithelial cells in feeding and moulting nymphs o...
18265077 - Preparation of myeloma cells.
17537857 - Enterovirus 70 receptor utilization is controlled by capsid residues that also regulate...
7505687 - Distinct effects of clinically used anthracycline antibiotics on ras oncogene-expressed...
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:  78     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  2004 Mar 
Date Detail:
Created Date:  2004-03-01     Completed Date:  2004-04-08     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2884-96     Citation Subset:  IM    
Affiliation:
Department of Pediatrics, University of Iowa College of Medicine, Iowa City, Iowa, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Cell Fusion*
Endocytosis / physiology*
Gene Expression Regulation, Viral*
Giant Cells
Hela Cells
Herpesvirus 3, Human / pathogenicity*,  physiology
Humans
Membrane Glycoproteins / genetics,  metabolism*
Mice
Microscopy, Confocal
Mutation
Viral Envelope Proteins / genetics,  metabolism*
Viral Proteins / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
AI22795/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Membrane Glycoproteins; 0/Viral Envelope Proteins; 0/Viral Proteins; 0/glycoprotein gp1, varicella-zoster virus; 0/gp 118 protein, Herpesvirus 3, Human
Comments/Corrections

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


Previous Document:  Bluetongue virus outer capsid proteins are sufficient to trigger apoptosis in mammalian cells.
Next Document:  Nodavirus coat protein imposes dodecahedral RNA structure independent of nucleotide sequence and len...