ArticleJournal of virology2018
Dimerization of Coronavirus nsp9 with Diverse Modes Enhances Its Nucleic Acid Binding Affinity.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- The Infectivity and Pathogenicity Characteristics of a Recombinant Porcine Epidemic Diarrhea Virus, CHFJFQ.Viruses · 2025Article
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- Nanobody against SARS-CoV-2 non-structural protein Nsp9 inhibits viral replication in human airway epithelia.Molecular therapy. Nucleic acids · 2024Article
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- Review
- Assessing nanobody interaction with SARS-CoV-2 Nsp9.PloS one · 2024Article
- Article
- Non-Structural Proteins (Nsp): A Marker for Detection of Human Coronavirus Families.Pathogens (Basel, Switzerland) · 2023Article
- Article
- Toll-like Receptor Mediation in SARS-CoV-2: A Therapeutic Approach.International journal of molecular sciences · 2022Review
- Two Years into the COVID-19 Pandemic: Lessons Learned.ACS infectious diseases · 2022Review
- Microscale Thermophoresis as a Tool to Study Protein Interactions and Their Implication in Human Diseases.International journal of molecular sciences · 2022Review
- Network for network concept offers new insights into host- SARS-CoV-2 protein interactions and potential novel targets for developing antiviral drugs.Computers in biology and medicine · 2022Review
- Functional mutations of SARS-CoV-2: implications to viral transmission, pathogenicity and immune escape.Chinese medical journal · 2022Article
- Article
- Predicted 3D model of the M protein of Porcine Epidemic Diarrhea Virus and analysis of its immunogenic potential.PloS one · 2022Article
- Targeting the Interaction Between Spike Protein and Nucleocapsid Protein for Suppression and Detection of Human Coronavirus OC43.Frontiers in immunology · 2022Article
- Structure of the multiple functional domains from coronavirus nonstructural protein 3.Emerging microbes & infections · 2021Article
- Structural, energetic and lipophilic analysis of SARS-CoV-2 non-structural protein 9 (NSP9).Scientific reports · 2021Article
- Genome composition and genetic characterization of SARS-CoV-2.Saudi journal of biological sciences · 2021Review
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9 authors.
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Abstract
Coronaviruses pose serious health threats to humans and other animals. Understanding the mechanisms of their replication has important implications for global health and economic stability. Nonstructural protein 9 (nsp9) is an essential RNA binding protein for coronavirus replication. However, the mechanisms of the dimerization and nucleic acid binding of nsp9 remain elusive. Here, we report four crystal structures, including wild-type porcine delta coronavirus (PDCoV) nsp9, PDCoV nsp9-ΔN7 (N-terminal 7 amino acids deleted), wild-type porcine epidemic diarrhea virus (PEDV) nsp9, and PEDV nsp9-C59A mutant. These structures reveal the diverse dimerization forms of coronavirus nsp9. We first found that the N-finger of nsp9 from PDCoV plays a critical role in dimerization. Meanwhile, PEDV nsp9 is distinguished by the presence of a disulfide bond in the dimer interface. Interestingly, size exclusion chromatography and analytical ultracentrifugation analyses indicate that the PDCoV nsp9-ΔN7 and PEDV nsp9-C59A mutants are monomeric in solution. In addition, electrophoretic mobility shift assays and microscale thermophoresis analysis indicate that the monomeric forms of PDCoV nsp9 and PEDV nsp9 still have nucleic acid binding affinity, although it is lower than that of the wild type. Our results show that the diverse dimerization forms of coronavirus nsp9 proteins enhance their nucleic acid binding affinity.
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