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The SARS-CoV-2 nucleocapsid protein (N protein) is a major internal structural component responsible for binding and packaging the viral RNA genome into ribonucleoprotein complexes, participating in virus assembly, and modulating host immune responses. It consists of N-terminal and C-terminal domains linked by a flexible, phosphorylated region and is highly immunogenic, making it a prominent target for diagnostics and antiviral strategies. The SARS-CoV-2 membrane protein (M protein) is the most abundant structural protein in the viral envelope, orchestrating virion assembly and morphology by scaffolding other viral proteins (N, S, E) and determining the shape and rigidity of the viral envelope. M protein forms dimers and oligomers, undergoes conformational changes, and interacts electrostatically with N protein and RNA; it is highly conserved and a key target for vaccine and antiviral development.
For N protein, inhibition of RNA binding or oligomerization can suppress viral replication. For M protein, inhibition of protein–protein interactions or oligomerization could prevent viral assembly.
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