Interaction of Sindbis virus with liposomal model membranes.
Radiolabeled Sindbis virus was found to bind to protein-free lipid model membranes (liposomes) derived from extracts of sheep erythrocytes. The virus interaction was dependent on initial pH, and the range of pH dependence (pH 6.0 to 6.8) was the same as the observed with virus-dependent hemagglutination. After the initial interaction, pH changes no longer influenced the virus binding to liposomes. Virus bound to liposomes prepared from a mixture of erythrocyte phospholipids, but the binding was greatly diminished when either cholesterol or phosphatidylethanolamine was omitted from the liposomal lipid mixture. It was concluded that phospholipids and cholesterol, in a bilayer configuration, may be sufficient for specific virus binding in the absence of membrane protein.
D000327:Adsorption; D000596:Amino Acids; D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000382:microbiology; D002499:Centrifugation, Density Gradient; D002784:Cholesterol; D004912:Erythrocytes / Q000276:immunology; D005777:Geese / Q000276:immunology; D006017:Glycolipids; D006387:Hemagglutination, Viral; D006863:Hydrogen-Ion Concentration; D008055:Lipids; D008081:Liposomes; D008954:Models, Biological; D010714:Phosphatidylethanolamines; D010743:Phospholipids; D012756:Sheep / Q000276:immunology; D012845:Sindbis Virus; D014316:Tritium
D000596:Amino Acids; D006017:Glycolipids; D008055:Lipids; D008081:Liposomes; D010714:Phosphatidylethanolamines; D010743:Phospholipids; D014316:Tritium; D002784:Cholesterol