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Interaction of viral envelope glycoproteins with fibronectin
Abstract:
An interaction between fibronectin and viral envelope glycoprotein micelles isolated from influenza A, parainfluenza 1, and mumps viruses was found by enzyme immunoassay. All three different glycoprotein micelles bound efficiently to solid-phase fibronectin. When fibronectin was permitted to bind to solid-phase viral glycoproteins, dose-dependent binding was observed. Soluble glycoprotein micelles inhibited the binding of fibronectin to immobilized glycoprotein preparations. The binding was not observed when fibronectin was pretreated with neuraminidase, suggesting that the sugar moieties of fibronectin are responsible for the affinity. This affinity may play a role in virus-cell interactions or in the opsonization of certain viruses during infection.
Insights
Fibronectin interacts with viral glycoproteins from influenza, parainfluenza, and mumps viruses. This binding, mediated by fibronectin
Area of Science:
- Virology
- Immunology
- Biochemistry
Background:
- Fibronectin is a key extracellular matrix protein involved in cell adhesion and immune responses.
- Viral envelope glycoproteins mediate virus entry into host cells and are targets for the immune system.
Purpose of the Study:
- To investigate the interaction between fibronectin and envelope glycoproteins from influenza A, parainfluenza 1, and mumps viruses.
- To elucidate the nature of the binding and the role of fibronectin's carbohydrate moieties in this interaction.
Main Methods:
- Enzyme immunoassay was used to detect and quantify the binding between fibronectin and viral glycoprotein micelles.
- Neuraminidase treatment was employed to assess the involvement of sugar residues in the interaction.
Main Results:
- All tested viral glycoprotein micelles efficiently bound to solid-phase fibronectin.
- Fibronectin binding to immobilized viral glycoproteins was dose-dependent.
- Soluble glycoprotein micelles inhibited this binding, and neuraminidase pretreatment of fibronectin abolished the interaction, indicating the role of sugar moieties.
Conclusions:
- A specific interaction exists between fibronectin and the envelope glycoproteins of influenza A, parainfluenza 1, and mumps viruses.
- This fibronectin-glycoprotein affinity is mediated by the carbohydrate components of fibronectin.
- This interaction may be significant in virus-host cell binding and viral opsonization during infections.