Abstract:
:The primary role of cytoplasmic viral RNA-dependent RNA polymerase (RdRp) is viral genome replication in the cellular cytoplasm. However, picornaviral RdRp denoted 3D polymerase (3D(pol)) also enters the host nucleus, where its function remains unclear. In this study, we describe a novel mechanism of viral attack in which 3D(pol) enters the nucleus through the nuclear localization signal (NLS) and targets the pre-mRNA processing factor 8 (Prp8) to block pre-mRNA splicing and mRNA synthesis. The fingers domain of 3D(pol) associates with the C-terminal region of Prp8, which contains the Jab1/MPN domain, and interferes in the second catalytic step, resulting in the accumulation of the lariat form of the splicing intermediate. Endogenous pre-mRNAs trapped by the Prp8-3D(pol) complex in enterovirus-infected cells were identified and classed into groups associated with cell growth, proliferation, and differentiation. Our results suggest that picornaviral RdRp disrupts pre-mRNA splicing processes, that differs from viral protease shutting off cellular transcription and translation which contributes to the pathogenesis of viral infection.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Liu YC,Kuo RL,Lin JY,Huang PN,Huang Y,Liu H,Arnold JJ,Chen SJ,Wang RY,Cameron CE,Shih SRdoi
10.1371/journal.ppat.1004199subject
Has Abstractpub_date
2014-06-26 00:00:00pages
e1004199issue
6eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-13-03244journal_volume
10pub_type
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