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Binding sites for rubella virus on erythrocyte membrane
P Mastromarino1, S Rieti, L Cioè
1Institute of Microbiology, School of Medicine, University of Rome, La Sapienza, Italy.
Archives of Virology
|January 1, 1989
Summary
Goose erythrocyte membranes contain lipid molecules, specifically phospholipids and glycolipids, that act as rubella virus (RV) receptors. These lipids are crucial for both viral attachment and fusion with host cells.
Area of Science:
- Virology
- Cell Biology
- Biochemistry
Background:
- Rubella virus (RV) requires specific cell surface receptors for entry.
- Identifying these receptors is key to understanding viral infection mechanisms.
Purpose of the Study:
- To identify the molecular components of goose erythrocyte membranes that function as rubella virus receptors.
- To elucidate the role of specific lipids in rubella virus attachment and fusion.
Main Methods:
- Isolation and solubilization of goose erythrocyte membranes.
- Assays for viral binding, fusion, hemagglutination, and hemolysis.
- Enzymatic (trypsin, neuraminidase, phospholipase A2) and chemical modifications of membrane components.
- Examination of purified lipid fractions and individual lipids.
Main Results:
- Solubilized membranes inhibited rubella virus attachment and fusion in a dose-dependent manner.
- Inhibitory activity was enhanced by trypsin/neuraminidase and abolished by phospholipase A2, suggesting lipid involvement.
- Lipid moieties, including phospholipids and glycolipids, were identified as inhibitors.
- Phosphatidylserine and cerebroside sulfate strongly inhibited hemagglutination and hemolysis.
- Specific phospholipids inhibited hemolysis but not binding, indicating distinct roles in fusion.
Conclusions:
- Cell surface receptors for rubella virus are primarily composed of membrane lipid molecules.
- Phospholipids and glycolipids, particularly phosphatidylserine and cerebroside sulfate, play critical roles in rubella virus-erythrocyte interactions.
- Different membrane lipids mediate distinct steps in the viral infection process, including attachment and fusion.