8YM1

Structure of SADS-CoV Virus Nucleocapsid Protein

Summary for 8YM1

• Entry DOI: 10.2210/pdb8ym1/pdb
• Descriptor: nucleocapsid phosphoprotein (2 entities in total)
• Functional Keywords: nucleocapsid protein, viral protein
• Biological source: Swine acute diarrhea syndrome coronavirus
• Total number of polymer chains: 8
• Total formula weight: 101146.27

Authors

Zhang, Y.,Wu, F.,Xu, W. (deposition date: 2024-03-08, release date: 2024-07-24, Last modification date: 2024-09-04)

Primary citation

Zhang, Y.,Wu, F.,Han, Y.,Wu, Y.,Huang, L.,Huang, Y.,Yan, D.,Jiang, X.,Ma, J.,Xu, W.
Unraveling the assembly mechanism of SADS-CoV virus nucleocapsid protein: insights from RNA binding, dimerization, and epitope diversity profiling.
J.Virol., 98:e0092624-e0092624, 2024

PubMed Abstract: The swine acute diarrhea syndrome coronavirus (SADS-CoV) has caused significant disruptions in porcine breeding and raised concerns about potential human infection. The nucleocapsid (N) protein of SADS-CoV plays a vital role in viral assembly and replication, but its structure and functions remain poorly understood. This study utilized biochemistry, X-ray crystallography, and immunization techniques to investigate the N protein's structure and function in SADS-CoV. Our findings revealed distinct domains within the N protein, including an RNA-binding domain, two disordered domains, and a dimerization domain. Through biochemical assays, we confirmed that the N-terminal domain functions as an RNA-binding domain, and the C-terminal domain is involved in dimerization, with the crystal structure analysis providing visual evidence of dimer formation. Immunization experiments demonstrated that the disordered domain 2 elicited a significant antibody response. These identified domains and their interactions are crucial for viral assembly. This comprehensive understanding of the N protein in SADS-CoV enhances our knowledge of its assembly and replication mechanisms, enabling the development of targeted interventions and therapeutic strategies.

PubMed: 39082816
DOI: 10.1128/jvi.00926-24

Experimental method

X-RAY DIFFRACTION (1.9 Å)