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The SARS-CoV-2 nucleocapsid protein antigen is the most abundant structural protein of the COVID-19 virus, encapsulating and packaging the viral RNA genome into ribonucleoprotein complexes within the viral particle[5][1][3]. It consists of an N-terminal RNA-binding domain and a C-terminal dimerization domain, connected by three intrinsically disordered regions[1][5][7]. Critical for viral replication, assembly, and immune evasion, the N protein also suppresses host stress granule assembly and modulates cellular responses[1]. Its conserved structure and high expression make it a primary antigen in rapid diagnostic tests and a promising experimental target for antiviral drug development[6][7]. Targeting its interaction with RNA or its post-translational modifications (such as methylation) can potentially inhibit SARS-CoV-2 infectivity[3][7], though no approved therapies directly target this protein. The N protein is also a major target of the host immune response and serves as a key biomarker for infection and disease status[6].
Inhibition of RNA binding: Prevents genome packaging and replication. Disruption of oligomerization: Impairs viral capsid assembly. Blocking post-translational modifications (e.g., methylation): Reduces viral RNA packaging.
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