Journal
VIRUSES-BASEL
Volume 8, Issue 2, Pages -Publisher
MDPI AG
DOI: 10.3390/v8020039
Keywords
enterovirus RNA replication; RNA replication complexes; MS2 hairpin; aptamer; ribonucleoprotein complexes; RNP isolation; RNA affinity
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Funding
- Comprehensive Cancer Center from the National Cancer Institute [P30CA062203]
- Public Health Service training grant from the National Institutes of Health [AI007319]
- Public Health Service grant from the National Institutes of Health [AI022693]
- BRS Shared Instrument grant from the Office of the Director, National Institutes of Health [1S10OD016328-01]
- California Center for Antiviral Drug Discovery (a Multicampus Research Program Initiative from the University of California)
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Despite being intensely studied for more than 50 years, a complete understanding of the enterovirus replication cycle remains elusive. Specifically, only a handful of cellular proteins have been shown to be involved in the RNA replication cycle of these viruses. In an effort to isolate and identify additional cellular proteins that function in enteroviral RNA replication, we have generated multiple recombinant polioviruses containing RNA affinity tags within the 3 or 5 noncoding region of the genome. These recombinant viruses retained RNA affinity sequences within the genome while remaining viable and infectious over multiple passages in cell culture. Further characterization of these viruses demonstrated that viral protein production and growth kinetics were unchanged or only slightly altered relative to wild type poliovirus. However, attempts to isolate these genetically-tagged viral genomes from infected cells have been hindered by high levels of co-purification of nonspecific proteins and the limited matrix-binding efficiency of RNA affinity sequences. Regardless, these recombinant viruses represent a step toward more thorough characterization of enterovirus ribonucleoprotein complexes involved in RNA replication.
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