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The SARS-CoV-2 Membrane (M) protein is the most abundant structural protein of the virus and is essential for viral assembly and morphogenesis (Source 1.2.1, 1.3.1). It is a type III transmembrane glycoprotein that coordinates the formation of the viral envelope by interacting with the Spike (S), Envelope (E), and Nucleocapsid (N) proteins (Source 1.3.2, 1.5.1). In the Omicron lineage, the M protein carries specific mutations, such as Q19E and A63T, which are thought to contribute to the variant's altered fitness and immune evasion capabilities (Source 1.3.3). Beyond its structural role, the M protein functions as an antagonist to the host's innate immune response by inhibiting interferon production, thereby facilitating viral replication (Source 1.3.1, 1.5.1). Recent breakthroughs have identified small-molecule inhibitors, such as JNJ-9676 and CIM-834, which target the M protein's conformational equilibrium to block viral particle formation (Source 1.2.1). As a highly conserved protein across variants, the M protein represents a promising therapeutic target for developing broad-spectrum antivirals that complement existing treatments targeting viral enzymes (Source 1.2.1, 1.3.3).
Inhibition of viral assembly and morphogenesis by disrupting M protein conformational states and its interactions with S, E, and N proteins.
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