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Matrix protein 1 of Influenza virus is the most abundant structural protein in influenza virions, forming an oligomeric matrix layer beneath the viral membrane. It provides essential mechanical stability, organizes the encapsidation of ribonucleoproteins, and regulates virus assembly, budding, and pH-driven disassembly during cell entry. M1 mediates interactions between internal viral components (vRNPs, NEP) and viral surface proteins (HA, NA, M2). Sequence-specific peptides from M1 are widely used as immunogenic epitopes in vaccine development and T-cell assays. Due to its central role in the virus life cycle and high conservation among strains, Matrix protein 1 is a promising, though currently unexploited, antiviral drug and immunotherapy target.
Drugs targeting M1 would aim to disrupt its ability to polymerize, oligomerize, or interact with ribonucleoprotein complexes or the viral membrane, preventing virus assembly and release. Immunotherapeutic strategies use M1-derived peptides (epitopes) for T-cell mediated immunity.
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