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Rotavirus interaction with isolated membrane vesicles

M C Ruiz¹, S R Alonso-Torre, A Charpilienne

¹Centre de Recherche sur l'Endocrinologie Moléculaire et le Développement, Centre Nationale de le Recherche Schientifique, Meudon, France.

Journal of Virology

|June 1, 1994

Summary

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Rotavirus outer capsid proteins destabilize cell membranes, causing fluorophore release. This membrane permeabilization is key to rotavirus entry into host cells.

Area of Science:

Virology
Cell Biology
Biochemistry

Background:

Rotavirus is a major cause of gastroenteritis in infants.
The mechanism of rotavirus epithelial cell infection is not fully understood.

Purpose of the Study:

To investigate the interaction of bovine rotavirus with pig enterocyte membrane vesicles.
To elucidate the role of viral proteins in membrane destabilization and infection.

Main Methods:

Using isolated enterocyte membrane vesicles loaded with fluorophores.
Monitoring fluorophore release (dequenching) upon incubation with purified rotavirus particles.
Analyzing the effect of trypsinized virions, salts, pH, temperature, and specific antibodies on dequenching kinetics.

Main Results:

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Trypsinized double-shelled rotavirions induced sigmoid-shaped fluorophore release, dependent on virus concentration, temperature, and pH.
Salt presence (100 mM) was essential for the reaction.
VP5* protein was identified as the active species, and Ca2+ inhibited the reaction.
Solubilization of the outer capsid altered kinetics and abolished Ca2+ inhibition.

Conclusions:

Rotavirus-induced membrane destabilization, mediated by trypsinized outer capsid proteins, leads to fluorophore release.
This membrane permeabilization mechanism is likely involved in rotavirus entry into host cells.
A hypothetical model for rotavirus-membrane interaction is proposed.