Document Detail


A single amino acid substitution in the cytoplasmic tail of the glycoprotein B of herpes simplex virus 1 affects both syncytium formation and binding to intracellular heparan sulfate.
MedLine Citation:
PMID:  12727347     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Herpes simplex virus 1 (HSV-1) (S) is a spontaneous syncytial mutant derived from the prototype HSV-1(F) after extensive plaque purification, and produces large syncytial plaques on Vero cells. Marker transfer experiments and DNA sequence analysis mapped the syncytial phenotype to a T-C base substitution at codon 787 of the cytoplasmic domain of mature gB, that results in Leu to Pro substitution and consequently belongs to the syn 3 locus. Both the cytoplasmic and the extracellular domains of gB are active in the fusion event since the addition of anti-gB monoclonal antibodies that recognize the extracellular domain of gB prevent HSV-1(S) induced cell fusion. Similarly, gD also participates in cell fusion since addition of anti-gD monoclonal antibodies also prevent HSV-1(S) induced cell fusion. Furthermore the glycoproteins B and D formed complexes in cells infected with mutant or wild type viruses. The amount of gB bound to total heparan sulfate is lower in the mutant than in the wild type strain. This difference becomes particularly profound when gB is associated with a portion of heparan sulfate intercalated to the membranes. The discrepancy in the binding of the mutant and wild type gB to heparan sulfate may be related to the mechanism of cell fusion induced by HSV-1(S).
Authors:
A Diakidi-Kosta; G Michailidou; G Kontogounis; A Sivropoulou; M Arsenakis
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Virus research     Volume:  93     ISSN:  0168-1702     ISO Abbreviation:  Virus Res.     Publication Date:  2003 May 
Date Detail:
Created Date:  2003-05-02     Completed Date:  2003-07-14     Revised Date:  2008-08-26    
Medline Journal Info:
Nlm Unique ID:  8410979     Medline TA:  Virus Res     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  99-108     Citation Subset:  IM    
Affiliation:
Laboratory of General Microbiology, Section of Genetics, Development and Molecular Biology, School of Biology, Aristotle University, Thessaloniki 54124, Greece.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acid Substitution
Animals
Antibodies, Monoclonal
Binding Sites
Cercopithecus aethiops
Chromatography, Affinity
Cytoplasm / virology
DNA, Viral / genetics,  isolation & purification
Giant Cells / physiology*
Heparitin Sulfate / metabolism*
Herpesvirus 1, Human / genetics*,  metabolism
Molecular Sequence Data
Point Mutation
Transfection
Vero Cells
Viral Envelope Proteins / chemistry,  genetics*,  isolation & purification
Chemical
Reg. No./Substance:
0/Antibodies, Monoclonal; 0/DNA, Viral; 0/Viral Envelope Proteins; 0/glycoprotein B, Simplexvirus; 9050-30-0/Heparitin Sulfate

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