Solubilized and cleaved VP7, the outer glycoprotein of rotavirus, induces permeabilization of cell membrane vesicles.
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.
Charpilienne
A
A
Laboratoire de Virologie et Immunologie Moléculaires INRA, C.R.J., Jouy-en-Josas, France.
Abad
M J
MJ
Michelangeli
F
F
Alvarado
F
F
Vasseur
M
M
Cohen
J
J
Ruiz
M C
MC
D000956:Antigens, Viral; D002213:Capsid / Q000502:physiology*; D036022:Capsid Proteins; D002463:Cell Membrane Permeability; D004533:Egtazic Acid / Q000494:pharmacology; D012401:Rotavirus / Q000378:metabolism*; D014357:Trypsin / Q000494:pharmacology
D000956:Antigens, Viral; D036022:Capsid Proteins; C060339:VP4 protein, Rotavirus; C050779:VP7 protein, Rotavirus; D004533:Egtazic Acid; D014357:Trypsin