ArticleThe FEBS journal2007
Expression, post-translational modification and biochemical characterization of proteins encoded by subgenomic mRNA8 of the severe acute respiratory syndrome coronavirus.
Article in The FEBS journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- UBR5 Acts as an Antiviral Host Factor against MERS-CoV via Promoting Ubiquitination and Degradation of ORF4b.Journal of virology · 2022Article
- Host-Genome Similarity Characterizes the Adaption of SARS-CoV-2 to Humans.Biomolecules · 2022Article
- Lost in deletion: The enigmatic ORF8 protein of SARS-CoV-2.Biochemical and biophysical research communications · 2021Review
- Exploring Virome Diversity in Public Data in South America as an Approach for Detecting Viral Sources From Potentially Emerging Viruses.Frontiers in genetics · 2021Article
- SARS-CoV-2 ORF8 and SARS-CoV ORF8ab: Genomic Divergence and Functional Convergence.Pathogens (Basel, Switzerland) · 2020Review
- The origin and underlying driving forces of the SARS-CoV-2 outbreak.Journal of biomedical science · 2020Article
- The Proteins of Severe Acute Respiratory Syndrome Coronavirus-2 (SARS CoV-2 or n-COV19), the Cause of COVID-19.The protein journal · 2020Review
- Identification of Novel Candidate Epitopes on SARS-CoV-2 Proteins for South America: A Review of HLA Frequencies by Country.Frontiers in immunology · 2020Review
- Origin and evolution of pathogenic coronaviruses.Nature reviews. Microbiology · 2019Review
- SARS-Coronavirus Open Reading Frame-8b triggers intracellular stress pathways and activates NLRP3 inflammasomes.Cell death discovery · 2019Article
- Post-translational modifications of coronavirus proteins: roles and function.Future virology · 2018Review
- Article
- Severe Acute Respiratory Syndrome (SARS) Coronavirus ORF8 Protein Is Acquired from SARS-Related Coronavirus from Greater Horseshoe Bats through Recombination.Journal of virology · 2015Article
- Article
- Accessory proteins of SARS-CoV and other coronaviruses.Antiviral research · 2014Review
- The role of severe acute respiratory syndrome (SARS)-coronavirus accessory proteins in virus pathogenesis.Viruses · 2012Review
- SARS coronavirus 8b reduces viral replication by down-regulating E via an ubiquitin-independent proteasome pathway.Microbes and infection · 2011Article
- Towards construction of viral vectors based on avian coronavirus infectious bronchitis virus for gene delivery and vaccine development.Journal of virological methods · 2009Article
- Translational control of the subgenomic RNAs of severe acute respiratory syndrome coronavirus.Virus genes · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The most striking difference between the subgenomic mRNA8 of severe acute respiratory syndrome coronavirus isolated from human and some animal species is the deletion of 29 nucleotides, resulting in splitting of a single ORF (ORF8) into two ORFs (ORF8a and ORF8b). ORF8a and ORF8b are predicted to encode two small proteins, 8a and 8b, and ORF8 a single protein, 8ab (a fusion form of 8a and 8b). To understand the functions of these proteins, we cloned cDNA fragments covering these ORFs into expression plasmids, and expressed the constructs in both in vitro and in vivo systems. Expression of a construct containing ORF8a and ORF8b generated only a single protein, 8a; no 8b protein expression was obtained. Expression of a construct containing ORF8 generated the 8ab fusion protein. Site-directed mutagenesis and enzymatic treatment revealed that protein 8ab is modified by N-linked glycosylation on the N81 residue and by ubiquitination. In the absence of the 8a region, protein 8b undergoes rapid degradation by proteasomes, and addition of proteasome inhibitors inhibits the degradation of protein 8b as well as the protein 8b-induced rapid degradation of the severe acute respiratory syndrome coronavirus E protein. Glycosylation could also stabilize protein 8ab. More interestingly, the two proteins could bind to monoubiquitin and polyubiquitin, suggesting the potential involvement of these proteins in the pathogenesis of severe acute respiratory syndrome coronavirus.
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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.