RT Journal Article
T1 Avian reovirus-triggered apoptosis enhances both virus spread and the processing of the viral nonstructural muNS protein
A1 Rodríguez Grille, Javier
A1 Busch, Lisa Kay
A1 Martínez Costas, José Manuel
A1 Benavente Martínez, Francisco Javier
K1 Avian reovirus
K1 muNS
K1 Apoptosis
K1 Caspase
K1 Proteolytic processing
K1 Viroplasms
K1 Virus spread
AB Avian reovirus non-structural protein muNS is partially cleaved in infected chicken embryo fibroblast cells to produce a 55-kDa carboxyterminal protein, termed muNSC, and a 17-kDa aminoterminal polypeptide, designated muNSN. In this study we demonstrate that muNS processing is catalyzed by a caspase 3-like protease activated during the course of avian reovirus infection. The cleavage site was mapped by site directed mutagenesis between residues Asp-154 and Ala-155 of the muNS sequence. Although muNS and muNSC, but not muNSN, are able to form inclusions when expressed individually in transfected cells, only muNS is able to recruit specific ARV proteins to these structures. Furthermore, muNSC associates with ARV factories more weakly than muNS, sigmaNS and lambdaA. Finally, the inhibition of caspase activity in ARV-infected cells does not diminish ARV gene expression and replication, but drastically reduces muNS processing and the release and dissemination of progeny viral particles
PB Elsevier
SN 0042-6822
YR 2014
FD 2014-08
LK http://hdl.handle.net/10347/18495
UL http://hdl.handle.net/10347/18495
LA eng
NO Rodríguez-Grille, J., Busch, L., Martínez-Costas, J., & Benavente, J. (2014). Avian reovirus-triggered apoptosis enhances both virus spread and the processing of the viral nonstructural muNS protein. Virology, 462-463, 49-59. doi: 10.1016/j.virol.2014.04.039
NO This work was funded by grants from the Ministerio de Economia Competitividad (BFU2010-22228) and from the Xunta de Galicia (CN 2012/018)
DS Minerva
RD 26 abr 2026