作者: Y. Ma , M. Anantpadma , J. M. Timpe , S. Shanmugam , S. M. Singh
DOI: 10.1128/JVI.01070-10
关键词:
摘要: Many aspects of the assembly hepatitis C virus (HCV) remain incompletely understood. To characterize role NS2 in production infectious virus, we determined interaction partners among other HCV proteins during productive infection. Pulldown assays showed that forms complexes with both structural and nonstructural proteins, including E1, E2, p7, NS3, NS5A. Confocal microscopy also demonstrated colocalizes NS5A dot-like structures near lipid droplets. However, did not coprecipitate E2 interacted only weakly NS3 pulldown assays. Also, there was no demonstrable between p7 or such Therefore, is uniquely capable interacting proteins. Among mutations NS2, prevent significantly reduced NS2-mediated protein interactions. These altered intracellular distribution appeared to modulate membrane topology C-terminal domain NS2. results suggest acts coordinate by mediating interactions envelope within replication adjacent droplets, where particle thought occur. may play an accessory regulating topology, which important for therefore function.