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Matrix protein 1 (M1) is the most abundant structural protein of the influenza A virus, including the highly pathogenic H7N9 subtype (UniProt, 2024). It forms a scaffold beneath the viral lipid envelope, providing structural stability and interacting with both the viral glycoproteins and the internal viral ribonucleoprotein (vRNP) complexes (Wikipedia, 2024). M1 plays a multifunctional role throughout the viral life cycle, facilitating viral uncoating during entry, regulating RNA transcription, and orchestrating the export of new vRNPs from the host nucleus to the assembly sites at the plasma membrane (Emerg Microbes Infect, 2025). In H7N9 viruses, specific mutations such as D156E in the M1 protein have been identified as critical determinants of viral morphology and respiratory droplet transmission in mammalian models (ASM Journals, 2019). Because M1 is highly conserved across influenza A subtypes, it is an attractive target for broad-spectrum antivirals, with experimental agents like the small-molecule 'wedge' PHE and siRNA-based AVI-7100 designed to disrupt viral assembly and budding (ResearchGate, 2025; PMC, 2015).
Inhibition of M1 self-oligomerization to disrupt viral assembly and budding; interference with the nuclear export of viral ribonucleoproteins (vRNPs); impairment of virion structural integrity and viral uncoating (Patsnap Synapse, 2024; ResearchGate, 2025).
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