ArticleVirology2012
Identification and characterization of Iflavirus 3C-like protease processing activities.
Article in Virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- New Iflavirus Species Characterized from Mosquitoes Captured in the Sao Paulo Zoological Facilities.Microorganisms · 2024Article
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- Diversity Analysis of Tick-Borne Viruses from Hedgehogs and Hares in Qingdao, China.Microbiology spectrum · 2023Article
- SARS-CoV-2 3CLpro whole human proteome cleavage prediction and enrichment/depletion analysis.Computational biology and chemistry · 2022Article
- Article
- Organization of the Structural Protein Region of La Jolla Virus Isolated from the Invasive Pest InsectViruses · 2021Article
- A Novel Rice Curl Dwarf-Associated Picornavirus Encodes a 3C Serine Protease Recognizing Uncommon EPT/S Cleavage Sites.Frontiers in microbiology · 2021Article
- Article
- ICTV Virus Taxonomy Profile: Iflaviridae.The Journal of general virology · 2017Article
- Complete genome of Chinese sacbrood virus from Apis cerana and analysis of the 3C-like cysteine protease.Virus genes · 2015Article
- Genetic characterization of a novel Iflavirus associated with vomiting disease in the Chinese oak silkmoth Antheraea pernyi.PloS one · 2014Article
- Characterization of a nodavirus replicase revealed a de novo initiation mechanism of RNA synthesis and terminal nucleotidyltransferase activity.The Journal of biological chemistry · 2013Article
- The nonstructural protein 2C of a Picorna-like virus displays nucleic acid helix destabilizing activity that can be functionally separated from its ATPase activity.Journal of virology · 2013Article
- Identification and characterization of RNA duplex unwinding and ATPase activities of an alphatetravirus superfamily 1 helicase.Virology · 2012Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viral replication and capsid assembly in the viruses in the order Picornavirales requires polyprotein proteolytic processing by 3C or 3C-like (3CL) proteases. We identified and characterized the 3CL protease of Ectropis obliqua virus (EoV) of the newly established family Iflaviridae (order Picornavirales). The bacterially expressed EoV 3CL protease domain autocatalytically released itself from larger precursors by proteolytic cleavage, and cleavage sites were determined via N-terminal sequencing of the cleavage products. This protease also mediated trans-proteolytic activity and cleaved the polyprotein at the same specific positions. Moreover, we determined the critical catalytic residues (H2261, D2299, C2383) for the protease activity, and characterized the biochemical properties of EoV 3CL and its responses to various protease inhibitors. Our work is the first study to identify an iflaviral 3CL protease and further characterize it in detail and should foster our understanding of EoV and other iflaviruses.
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