Interactions of Semliki Forest virus spike glycoprotein rosettes and vesicles with cultured cells.
Semliki Forest virus (SFV)-derived spike glycoprotein rosettes (soluble octameric complexes), virosomes (lipid vesicles with viral spike glycoproteins), and liposomes (protein-free lipid vesicles) have been used to investigate the interaction of subviral particles with BHK-21 cells. Cell surface binding, internalization, degradation, and low pH-dependent membrane fusion were quantitatively determined. Electron microscopy was used to visualize the interactions. Virosomes and rosettes, but not liposomes, bound to cells. Binding occurred preferentially to microvilli and was inhibited by added SFV; it increased with decreasing pH but was, in all cases, less efficient than intact virus. At 37 degrees C the cell surface-bound rosettes and virosomes were internalized via coated pits and coated vesicles. After a lag period of 45 min the protein components of the internalized ligands were degraded and appeared, as acid-soluble activity, in the medium. The uptake of rosettes and virosomes was found to be similar to the adsorptive endocytosis of SFV except that their average residence times on the cell surface were longer. The rosettes and the liposomes did not show low pH-induced membrane fusion activity. The virosomes, however, irrespective of the lipid compositions used, displayed hemolytic activity at mildly acidic pH and were able to fuse with the plasma membrane of cells with an efficiency of 0.25 that observed with intact viruses. Cell-cell fusion activity was not observed with any of the subviral components. The results indicated that subviral components possess some of the entry properties of the intact virus.
D000818:Animals; D002462:Cell Membrane / Q000502:physiology; D002478:Cells, Cultured; D006224:Cricetinae; D004705:Endocytosis; D006023:Glycoproteins / Q000502:physiology; D006863:Hydrogen-Ion Concentration; D008081:Liposomes; D008561:Membrane Fusion; D011991:Receptors, Virus / Q000502:physiology*; D012397:Rosette Formation; D012672:Semliki forest virus / Q000502:physiology* / Q000648:ultrastructure; D014764:Viral Proteins / Q000502:physiology*
D006023:Glycoproteins; D008081:Liposomes; D011991:Receptors, Virus; D014764:Viral Proteins