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Influenza A virus matrix protein 1 (M1) is the most abundant structural protein in the influenza A virion, forming a continuous layer beneath the viral lipid envelope to provide mechanical stability and determine the shape of the virus particle [1, 4]. It plays a multifaceted role throughout the viral life cycle, including the uncoating of the virus during entry, the nuclear export of viral ribonucleoproteins (vRNPs), and the coordination of viral assembly and budding at the host cell membrane [1, 3, 15]. Because M1 is highly conserved across diverse influenza A subtypes (such as H1N1, H3N2, and H5N1), its T-cell epitopes are considered prime targets for the development of universal influenza vaccines [5, 7, 21]. These vaccines aim to induce cross-reactive CD4+ and CD8+ T-cell responses that can recognize and clear infected cells regardless of the antigenic drift seen in surface proteins like hemagglutinin [8, 19]. While M1 is an internal protein, it is processed and presented by MHC molecules on the surface of infected cells, making it accessible to the cellular immune system [17, 21].
Induction of cross-reactive CD4+ and CD8+ T-cell mediated immunity to clear virus-infected cells.
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