Solubilized and cleaved VP7, the outer glycoprotein of rotavirus, induces permeabilization of cell membrane vesicles

• Published in: Journal of general virology Vol. 78; no. 6; pp. 1367 - 1371
• Main Authors: Charpilienne, A, Abad, MJ, Michelangeli, F, Alvarado, F, Vasseur, M, Cohen, J, Ruiz, MC
• Format: Journal Article
• Language: English
• Published: England Soc General Microbiol 01.06.1997
• Subjects: Antigens, Viral; Capsid - physiology; Capsid Proteins; Cell Membrane Permeability; Egtazic Acid - pharmacology; Rotavirus - metabolism; Trypsin - pharmacology
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-78-6-1367

A Charpilienne, MJ Abad, F Michelangeli, F Alvarado, M Vasseur, J Cohen and MC Ruiz Laboratoire de Virologie et Immunologie Moleculaires INRA, C.R.J., Jouy- en-Josas, France. It has been previously shown that rotavirus triple-layered particles induce permeabilization of liposomes and membrane vesicles. These effects were mediated by one or both of the solubilized outer-capsid proteins, VP4 and VP7. Permeabilization was dependent on trypsin treatment of the viral particles, suggesting that VP4 was involved. To analyse the respective roles of the outer-capsid proteins in this permeabilization process, we have used membrane vesicles loaded with carboxyfluorescein and virus-like particles derived from insect cells co-expressing various sets of capsid proteins. Virus-like particles containing VP2, VP6 and VP7 (VLP2/6/7) are as efficient in permeabilizing vesicles as triple-layered particles. As with double- layered particles, virus-like particles made of VP2 and VP6 had no effect on vesicle permeabilization. Permeabilization of membrane vesicles required trypsinization of the VP7 solubilized from VLP2/6/7. These results show that solubilized and trypsinized VP7 is able to induce membrane permeabilization, independently of the presence of VP4.