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Influenza matrix protein 1 (M1) is the most abundant structural protein of the influenza A virus, forming a continuous layer beneath the viral lipid envelope [1, 2]. It serves as a multifunctional adapter that orchestrates several critical stages of the viral lifecycle, including viral uncoating, genome transcription, nuclear export of viral ribonucleoproteins (vRNPs), and the assembly and budding of new virions [2, 3, 6]. M1 is highly conserved across different influenza A subtypes, making it a prime candidate for the development of universal vaccines and broad-spectrum antivirals that could overcome the resistance issues associated with current neuraminidase and M2 ion channel inhibitors [1, 20, 24]. Experimental small molecules, such as the "wedge" inhibitor PHE and the stabilizer M1m1, have demonstrated the potential to halt viral replication by interfering with M1's ability to self-associate or by blocking}
Inhibition of viral assembly and budding through disruption of M1 self-oligomerization; interference with the nuclear export of viral ribonucleoproteins (vRNPs); and stabilization of the M1 layer to prevent pH-dependent uncoating.
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