Document Detail


The role of the ganglioside GD1a as a receptor for Sendai virus.
MedLine Citation:
PMID:  7827024     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The ganglioside GD1a, which serves as a receptor for Sendai virus, also affects lipid polymorphism as determined by 31P nuclear magnetic resonance. The ganglioside promotes the formation of isotropic structures in monomethyldioleoylphosphatidylethanolamine. GD1a also raises the bilayer to hexagonal phase transition temperature of this lipid. The effects of GD1a on the kinetics of viral fusion can be understood on the basis of its role in facilitating the binding of Sendai virus to target membranes as well as its effects on membrane physical properties. Fusion of Sendai virus with liposomes composed of egg phosphatidylethanolamine is particularly sensitive to the presence of ganglioside. In the absence of ganglioside no fusion is observed due to the absence of virus binding to the target membrane. Between 2 and 6 mol % GD1a in egg phosphatidylethanolamine liposomes there is a marked increase in the rate constant of binding of the virus to the liposome but a decrease in the fusion rate constant. The latter effect is found to be common to a number of other amphiphiles that raise the bilayer to hexagonal phase transition temperature. The ganglioside enhances virus binding to liposomes of all the compositions studied, but leakage rates and fusion rate constants are either unaffected or reduced. In the systems studied, the enhanced formation of isotropic structures in liposomes containing the ganglioside does not enhance the kinetics of the actual fusion reaction.
Authors:
R M Epand; S Nir; M Parolin; T D Flanagan
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  34     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1995 Jan 
Date Detail:
Created Date:  1995-02-23     Completed Date:  1995-02-23     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1084-9     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
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MeSH Terms
Descriptor/Qualifier:
Gangliosides / metabolism*
HN Protein / metabolism
Liposomes
Membrane Fusion
Membrane Lipids / chemistry
Parainfluenza Virus 1, Human / metabolism*
Phosphatidylethanolamines / chemistry
Receptors, Virus / chemistry*
Viral Fusion Proteins / metabolism
Chemical
Reg. No./Substance:
0/Gangliosides; 0/HN Protein; 0/Liposomes; 0/Membrane Lipids; 0/Phosphatidylethanolamines; 0/Receptors, Virus; 0/Viral Fusion Proteins; 12707-58-3/ganglioside, GD1a

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


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