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Electron microscopic study on the interaction of Sendai virus with liposomes containing glycophorin
Abstract:
The interaction of liposomes containing glycophorin, a major sialoglycoprotein of human erythrocytes, with Sendai virus was studied by freeze-fractures and negative staining electron-microscopy. Viral envelopes were absorbed on liposomal membranes at 0 degrees C. When the temperature was shifted up to 37 degrees C, the viral envelopes fused with the liposomal membranes (envelope fusion). Particles representing viral membrane components formed clusters on liposomal membranes after incubation for more than 1 h at 37 degrees C.
Insights
Sendai virus interacts with liposomes containing glycophorin, a human erythrocyte sialoglycoprotein. Upon warming, viral envelopes fuse with liposomal membranes, and viral components cluster on the liposomes.
Area of Science:
- Biophysics
- Membrane Biology
- Virology
Background:
- Glycophorin is a major sialoglycoprotein in human red blood cell membranes.
- Sendai virus is a paramyxovirus known for its membrane fusion capabilities.
Purpose of the Study:
- To investigate the interaction between Sendai virus and liposomes containing glycophorin.
- To elucidate the mechanism of viral envelope fusion with liposomal membranes.
Main Methods:
- Freeze-fracture electron microscopy
- Negative staining electron microscopy
Main Results:
- Sendai virus envelopes adsorbed to glycophorin-containing liposomes at 0°C.
- Viral envelope fusion with liposomal membranes occurred at 37°C.
- Viral membrane components aggregated on liposomal surfaces after prolonged incubation.
Conclusions:
- Sendai virus can fuse with liposomes incorporating glycophorin.
- This fusion process involves the integration and subsequent clustering of viral membrane components.