Rhinovirus infection inhibited nuclear import and caused the degradation of nuclear pore complex components Nup153 and p62, resulting in the cytoplasmic accumulation of nuclear proteins.
Rhinovirus inhibits nuclear import and degrades NPC components, suggesting a common picornavirus strategy to evade host immune defenses and accumulate nuclear proteins in the cytoplasm.
Nucleocytoplasmic trafficking pathways and the status of nuclear pore complex (NPC) components were examined in cells infected with rhinovirus type 14. A variety of shuttling and nonshuttling nuclear proteins, using multiple nuclear import pathways, accumulated in the cytoplasm of cells infected with rhinovirus. An in vitro nuclear import assay with semipermeabilized infected cells confirmed that nuclear import was inhibited and that docking of nuclear import receptor-cargo complexes at the cytoplasmic face of the NPC was prevented in rhinovirus-infected cells. The relocation of cellular proteins and inhibition of nuclear import correlated with the degradation of two NPC components, Nup153 and p62. The degradation of Nup153 and p62 was not due to induction of apoptosis, because p62 was not proteolyzed in apoptotic HeLa cells, and Nup153 was cleaved to produce a 130-kDa cleavage product that was not observed in cells infected with poliovirus or rhinovirus. The finding that both poliovirus and rhinovirus cause inhibition of nuclear import and degradation of NPC components suggests that this may be a common feature of the replicative cycle of picornaviruses. Inhibition of nuclear import is predicted to result in the cytoplasmic accumulation of a large number of nuclear proteins that could have functions in viral translation, RNA synthesis, packaging, or assembly. Additionally, inhibition of nuclear import also presents a novel strategy whereby cytoplasmic RNA viruses can evade host immune defenses by preventing signal transduction into the nucleus.
Gustin et al. (Sun,) conducted a other in Rhinovirus infection. Rhinovirus type 14 infection vs. Mock infection was evaluated on Nuclear import activity and degradation of NPC components (Nup153 and p62). Rhinovirus infection inhibited nuclear import and caused the degradation of nuclear pore complex components Nup153 and p62, resulting in the cytoplasmic accumulation of nuclear proteins.