TY - JOUR
T1 - Structural Insights of the SARS-CoV-2 Nucleocapsid Protein
T2 - Implications for the Inner-workings of Rapid Antigen Tests
AU - Casasanta, Michael A.
AU - Jonaid, G. M.
AU - Kaylor, Liam
AU - Luqiu, William Y.
AU - Dicecco, Liza Anastasia
AU - Solares, Maria J.
AU - Berry, Samantha
AU - Dearnaley, William J.
AU - Kelly, Deborah F.
N1 - Publisher Copyright:
© 2022 The Author(s). Published by Oxford University Press on behalf of the Microscopy Society of America. All rights reserved.
PY - 2023/4/1
Y1 - 2023/4/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85172254010&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85172254010&partnerID=8YFLogxK
U2 - 10.1093/micmic/ozac036
DO - 10.1093/micmic/ozac036
M3 - Article
C2 - 37749713
AN - SCOPUS:85172254010
SN - 1431-9276
VL - 29
SP - 649
EP - 657
JO - Microscopy and Microanalysis
JF - Microscopy and Microanalysis
IS - 2
ER -