RT Journal Article SR Electronic(1) A1 Charpilienne, A A1 Abad, M J A1 Michelangeli, F A1 Alvarado, F A1 Vasseur, M A1 Cohen, J A1 Ruiz, M CYR 1997 T1 Solubilized and cleaved VP7, the outer glycoprotein of rotavirus, induces permeabilization of cell membrane vesicles. JF Journal of General Virology, VO 78 IS 6 SP 1367 OP 1371 DO https://doi.org/10.1099/0022-1317-78-6-1367 PB Microbiology Society, SN 1465-2099, AB It has been previously shown that rotavirus triplelayered 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-78-6-1367