ArticleJournal of virology1998
Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: identification of a papain-like proteinase and its substrate.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 57 citations in OpenAlex.
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- Dimerization of Coronavirus nsp9 with Diverse Modes Enhances Its Nucleic Acid Binding Affinity.Journal of virology · 2018Article
- Functional analyses of the three simian hemorrhagic fever virus nonstructural protein 1 papain-like proteases.Journal of virology · 2014Article
- Targeting membrane-bound viral RNA synthesis reveals potent inhibition of diverse coronaviruses including the middle East respiratory syndrome virus.PLoS pathogens · 2014Article
- Molecular modeling and analysis of hepatitis E virus (HEV) papain-like cysteine protease.Virus research · 2014Article
- Papain-like protease 1 from transmissible gastroenteritis virus: crystal structure and enzymatic activity toward viral and cellular substrates.Journal of virology · 2010Article
- Exchange of the coronavirus replicase polyprotein cleavage sites alters protease specificity and processing.Journal of virology · 2010Article
- Variable oligomerization modes in coronavirus non-structural protein 9.Journal of molecular biology · 2008Article
- Human coronavirus 229E papain-like proteases have overlapping specificities but distinct functions in viral replication.Journal of virology · 2007Article
- Article
- Differential role of N-terminal polyprotein processing in coronavirus genome replication and minigenome amplification.Advances in experimental medicine and biology · 2006Article
- The coronavirus replicase: insights into a sophisticated enzyme machinery.Advances in experimental medicine and biology · 2006Review
- The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity.Journal of virology · 2005Article
- A point mutation within the replicase gene differentially affects coronavirus genome versus minigenome replication.Journal of virology · 2005Article
- Inhibition of SARS-CoV 3C-like Protease Activity by Theaflavin-3,3'-digallate (TF3).Evidence-based complementary and alternative medicine : eCAM · 2005Article
- Mining SARS-CoV protease cleavage data using non-orthogonal decision trees: a novel method for decisive template selection.Bioinformatics (Oxford, England) · 2005Article
- Viral and cellular proteins involved in coronavirus replication.Current topics in microbiology and immunology · 2005Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Expression of the coronavirus gene 1-encoded polyproteins, pp1a and pp1ab, is linked to a series of proteolytic events involving virus-encoded proteinases. In this study, we used transfection and immunoprecipitation assays to show that the human coronavirus 229E-encoded papain-like cysteine proteinase, PCP1, is responsible for the release of an amino-terminal protein, p9, from the gene 1-encoded polyproteins. The same protein, p9, has also been identified in virus-infected cells. Furthermore, using an in vitro trans-cleavage assay, we defined the proteolytic cleavage site at the carboxyl terminus of p9 as pp1a-pp1ab amino acids Gly-111 and Asn-112. These results and a comparative sequence analysis suggest that substrate positions P1 and P5 seem to be the major determinants of the PCP1 cleavage site and that the latter can occupy a variable position at the amino terminus of the coronavirus ppla and pplab polyproteins. By combining the trans-cleavage assay with deletion mutagenesis, we were also able to locate the boundaries of the active PCP1 domain between pp1a-pp1ab amino acids Gly-861-Glu-975 and Asn-1209-Gln-1285. Finally, codon mutagenesis was used to show that Cys-1054 and His-1205 are essential for PCP1 proteolytic activity, suggesting that these amino acids most likely have a catalytic function.
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