ArticleVirus research1999
Activity of a purified His-tagged 3C-like proteinase from the coronavirus infectious bronchitis virus.
Article in Virus research, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Expression, purification, and in vitro activity of an arterivirus main proteinase.Virus research · 2006Article
- Mining SARS-CoV protease cleavage data using non-orthogonal decision trees: a novel method for decisive template selection.Bioinformatics (Oxford, England) · 2005Article
- The coronavirus replicase.Current topics in microbiology and immunology · 2005Review
- Membrane association and dimerization of a cysteine-rich, 16-kilodalton polypeptide released from the C-terminal region of the coronavirus infectious bronchitis virus 1a polyprotein.Journal of virology · 2002Article
- Reverse genetics system for the avian coronavirus infectious bronchitis virus.Journal of virology · 2001Article
- Further characterization of the coronavirus infectious bronchitis virus 3C-like proteinase and determination of a new cleavage site.Virology · 2000Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Previous studies in vitro of the processing of cloned polyprotein fragments from the coronavirus infectious bronchitis virus (IBV) large open reading frame (ORF1), confirmed the activity of a predicted 3C-like proteinase (3CLP) domain and suggested that the proteinase is released autocatalytically from the polyprotein in the form of a 35 kDa protein, 3CLpro, capable of further cleavages in trans. In order to identify such cleavages within the ORF1 polyprotein mediated by 3CLpro, the proteinase was expressed in bacteria, purified and used in trans cleavage assays with polyprotein fragments lacking the 3CLP domain as targets. The proteinase was expressed as a polyprotein fragment which was able to process during expression in bacterial cells, releasing mature 3CLpro. A histidine (His6) tag was introduced close to the C-terminus of the proteinase to aid purification. Processing demonstrated by the tagged proteinase was indistinguishable from that of the wild-type enzyme indicating that the site chosen for the tag was permissive. From these studies we were able to demonstrate trans cleavages consistent with the use of most of the previously predicted or identified sites within the open reading frame of gene 1. This tentatively completes the processing map for the ORF1 region with respect to 3CLpro.
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