ArticleThe Journal of biological chemistry2008
The two-component NS2B-NS3 proteinase represses DNA unwinding activity of the West Nile virus NS3 helicase.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 53 citations in OpenAlex.
- West Nile virus unmasked: from gene variability to future challenges.Frontiers in cellular and infection microbiology · 2025Review
- Identifying Allosteric Small-Molecule Binding Sites of Inactive NS2B-NS3 Proteases of PathogenicViruses · 2024Article
- Dual function of Zika virus NS2B-NS3 protease.PLoS pathogens · 2023Article
- Flavivirus proteases: The viral Achilles heel to prevent future pandemics.Antiviral research · 2023Review
- Mechanical regulation of the helicase activity of Zika virus NS3.Biophysical journal · 2022Article
- Review
- Review
- Review
- Potential Dual Role of West Nile Virus NS2B in Orchestrating NS3 Enzymatic Activity in Viral Replication.Viruses · 2021Article
- Degradation of MicroRNA miR-466d-3p by Japanese Encephalitis Virus NS3 Facilitates Viral Replication and Interleukin-1β Expression.Journal of virology · 2020Article
- Zika virus NS3 is a canonical RNA helicase stimulated by NS5 RNA polymerase.Nucleic acids research · 2019Article
- NS3 helicase from dengue virus specifically recognizes viral RNA sequence to ensure optimal replication.Nucleic acids research · 2017Article
- Uncoupling of ProteaseJournal of virology · 2017Article
- Programmed ribosomal frameshift alters expression of west nile virus genes and facilitates virus replication in birds and mosquitoes.PLoS pathogens · 2014Article
- Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.Virologica Sinica · 2014Review
- Functional cross-talk between distant domains of chikungunya virus non-structural protein 2 is decisive for its RNA-modulating activity.The Journal of biological chemistry · 2014Article
- West Nile virus drug discovery.Viruses · 2013Review
- The interdomain interface in bifunctional enzyme protein 3/4A (NS3/4A) regulates protease and helicase activities.Protein science : a publication of the Protein Society · 2013Article
- Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function.Nature chemical biology · 2012Article
- Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Similar to many flavivirus types including Dengue and yellow fever viruses, the nonstructural NS3 multifunctional protein of West Nile virus (WNV) with an N-terminal serine proteinase domain and an RNA triphosphatase, an NTPase domain, and an RNA helicase in the C-terminal domain is implicated in both polyprotein processing and RNA replication and is therefore a promising drug target. To exhibit its proteolytic activity, NS3 proteinase requires the presence of the cofactor encoded by the upstream NS2B sequence. During our detailed investigation of the biology of the WNV helicase, we characterized the ATPase and RNA/DNA unwinding activities of the full-length NS2B-NS3 proteinase-helicase protein as well as the individual NS3 helicase domain lacking both the NS2B cofactor and the NS3 proteinase sequence and the individual NS3 proteinase-helicase lacking only the NS2B cofactor. We determined that both the NS3 helicase and NS3 proteinase-helicase constructs are capable of unwinding both the DNA and the RNA templates. In contrast, the full-length NS2B-NS3 proteinase-helicase unwinds only the RNA templates, whereas its DNA unwinding activity is severely repressed. Our data suggest that the productive, catalytically competent fold of the NS2B-NS3 proteinase moiety represents an essential component of the RNA-DNA substrate selectivity mechanism in WNV and, possibly, in other flaviviruses. Based on our data, we hypothesize that the mechanism we have identified plays a role yet to be determined in WNV replication occurring both within the virus-induced membrane-bound replication complexes in the host cytoplasm and in the nuclei of infected cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.