ArticleProtein science : a publication of the Protein Society2009
Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 30 citations in OpenAlex.
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- Positive selection, genetic recombination, and intra-host evolution in novel equine coronavirus genomes and other members of theMicrobiology spectrum · 2024Article
- Structural proteins of human coronaviruses: what makes them different?Frontiers in cellular and infection microbiology · 2024Review
- Cell surface nucleocapsid protein expression: A betacoronavirus immunomodulatory strategy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cell Surface Nucleocapsid Protein Expression: A Betacoronavirus Immunomodulatory Strategy.bioRxiv : the preprint server for biology · 2023Article
- Review
- Comparing the Nucleocapsid Proteins of Human Coronaviruses: Structure, Immunoregulation, Vaccine, and Targeted Drug.Frontiers in molecular biosciences · 2022Review
- High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2.Biochemical and biophysical research communications · 2021Article
- Molecular determinants of Ebola nucleocapsid stability from molecular dynamics simulations.The Journal of chemical physics · 2020Article
- Research Progress on Coronavirus Prevention and Control in Animal-Source Foods.Journal of multidisciplinary healthcare · 2020Review
- An in vivo cell-based assay for investigating the specific interaction between the SARS-CoV N-protein and its viral RNA packaging sequence.Biochemical and biophysical research communications · 2019Article
- Interaction of coronavirus nucleocapsid protein with the 5'- and 3'-ends of the coronavirus genome is involved in genome circularization and negative-strand RNA synthesis.The FEBS journal · 2019Article
- microRNAs in viral acute respiratory infections: immune regulation, biomarkers, therapy, and vaccines.ExRNA · 2019Review
- Recent insights into the development of therapeutics against coronavirus diseases by targeting N protein.Drug discovery today · 2016Review
- Crystallographic analysis of the N-terminal domain of Middle East respiratory syndrome coronavirus nucleocapsid protein.Acta crystallographica. Section F, Structural biology communications · 2015Article
- The cellular interactome of the coronavirus infectious bronchitis virus nucleocapsid protein and functional implications for virus biology.Journal of virology · 2013Article
- Crystal structure-based exploration of the important role of Arg106 in the RNA-binding domain of human coronavirus OC43 nucleocapsid protein.Biochimica et biophysica acta · 2013Article
- Evolution of infectious bronchitis virus in Taiwan: positively selected sites in the nucleocapsid protein and their effects on RNA-binding activity.Veterinary microbiology · 2013Article
- Immunoreactivity characterisation of the three structural regions of the human coronavirus OC43 nucleocapsid protein by Western blot: implications for the diagnosis of coronavirus infection.Journal of virological methods · 2013Article
- Oligomerization of the carboxyl terminal domain of the human coronavirus 229E nucleocapsid protein.FEBS letters · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human coronavirus OC43 (HCoV-OC43) is one of the causes of the "common cold" in human during seasons of cold weather. The primary function of the HCoV-OC43 nucleocapsid protein (N protein) is to recognize viral genomic RNA, which leads to ribonucleocapsid formation. Here, we characterized the stability and identified the functional regions of the recombinant HCoV-OC43 N protein. Circular dichroism and fluorescence measurements revealed that the HCoV-OC43 N protein is more highly ordered and stabler than the SARS-CoV N protein previously studied. Surface plasmon resonance (SPR) experiments showed that the affinity of HCoV-OC43 N protein for RNA was approximately fivefold higher than that of N protein for DNA. Moreover, we found that the HCoV-OC43 N protein contains three RNA-binding regions in its N-terminal region (residues 1-173) and central-linker region (residues 174-232 and 233-300). The binding affinities of the truncated N proteins and RNA follow the order: residues 1-173-residues 233-300 > residues 174-232. SPR experiments demonstrated that the C-terminal region (residues 301-448) of HCoV-OC43 N protein lacks RNA-binding activity, while crosslinking and gel filtration analyses revealed that the C-terminal region is mainly involved in the oligomerization of the HCoV-OC43 N protein. This study may benefit the understanding of the mechanism of HCoV-OC43 nucleocapsid formation.
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