Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease.

摘要: Previous work has shown that several nucleoporins, including Nup62 are degraded in cells infected with human rhinovirus (HRV) and poliovirus (PV) this contributes to the disruption of certain nuclear transport pathways. In study, mechanisms underlying proteolysis have been investigated. Analysis lysates from HRV-infected revealed was cleaved at multiple sites during viral infection. The addition purified HRV2 2A protease (2Apro) uninfected HeLa whole cell resulted cleavage Nup62, suggesting 2Apro is a major contributor processing. ability cleave bacterially expressed demonstrated directly cleaves vitro. Site-directed mutagenesis putative identified six different positions by This analysis were located between amino acids 103 298 suggested N-terminal FG-rich region released pore complex cells. HRV- PV-infected using domain-specific antibodies confirmed indeed case. These results consistent model whereby PV HRV disrupt nucleo-cytoplasmic trafficking selectively removing FG repeat domains subset proteins.