8FG2

SARS-CoV-2 Nucleocapsid dimer structure determined from COVID-19 patients

Summary for 8FG2

• Entry DOI: 10.2210/pdb8fg2/pdb
• EMDB information: 29072
• Descriptor: Nucleoprotein (1 entity in total)
• Functional Keywords: sars-cov-2, n protein, covid-19, rna binding protein, viral protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 91379.29

Authors

Casasanta, M.,Jonaid, G.M.,Kaylor, L.,Luqiu, W.,DiCecco, L.,Solares, M.,Berry, S.,Kelly, D.F. (deposition date: 2022-12-12, release date: 2023-01-11, Last modification date: 2023-10-11)

Primary citation

Casasanta, M.A.,Jonaid, G.M.,Kaylor, L.,Luqiu, W.Y.,DiCecco, L.A.,Solares, M.J.,Berry, S.,Dearnaley, W.J.,Kelly, D.F.
Structural Insights of the SARS-CoV-2 Nucleocapsid Protein: Implications for the Inner-workings of Rapid Antigen Tests.
Microsc Microanal, 29:649-657, 2023

PubMed Abstract: The nucleocapsid (N) protein is an abundant component of SARS-CoV-2 and a key analyte for lateral-flow rapid antigen tests. Here, we present new structural insights for the SARS-CoV-2 N protein using cryo-electron microscopy (EM) and molecular modeling tools. Epitope mapping based on structural data supported host-immune interactions in the C-terminal portion of the protein, while other regions revealed protein-protein interaction sites. Complementary modeling results suggested that N protein structures from known variants of concern (VOC) are nearly 100% conserved at specific antibody-binding sites. Collectively, these results suggest that rapid tests that target the nucleocapsid C-terminal domain should have similar accuracy across all VOCs. In addition, our combined structural modeling workflow may guide the design of immune therapies to counter viral processes as we plan for future variants and pandemics.

PubMed: 37749713
DOI: 10.1093/micmic/ozac036

Experimental method

ELECTRON MICROSCOPY (6 Å)