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Influenza B virus (IBV) antigens are the structural and functional proteins of the influenza B virus that serve as primary targets for both the host immune system and pharmacological interventions [2, 6]. The most prominent targets are the surface glycoproteins, hemagglutinin (HA), which mediates viral attachment and entry into host cells, and neuraminidase (NA), which facilitates the release of progeny virions by cleaving sialic acid residues [1, 13, 20]. Other critical antigens include the nucleoprotein (NP) and the viral polymerase subunits (PA, PB1, and PB2), which are essential for genome replication and transcription [6, 19]. These proteins are the central components of seasonal influenza vaccines, designed to elicit neutralizing antibodies that provide protection against circulating lineages such as B/Victoria and B/Yamagata [15, 17]. Therapeutic agents, including neuraminidase inhibitors like oseltamivir and zanamivir, as well as polymerase inhibitors like baloxavir marboxil, interact with these specific antigens to disrupt the viral life cycle and reduce disease burden [1, 11, 16]. The continuous evolution of these antigens through antigenic drift remains a significant challenge, necessitating annual vaccine reformulations and monitoring for emergent drug resistance [7, 21].
Inhibition of the viral neuraminidase enzyme to prevent progeny virion release from host cells; inhibition of the cap-dependent endonuclease within the polymerase acidic (PA) subunit to block viral mRNA synthesis; and antibody-mediated neutralization of hemagglutinin to prevent viral attachment and entry.
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