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Lassa virus antigens represent the essential structural and functional proteins of the Lassa virus (LASV), the causative agent of Lassa fever, a severe hemorrhagic illness endemic to West Africa. The primary therapeutic targets include the Glycoprotein Complex (GPC), the Nucleoprotein (NP), and the Large (L) protein [2, 18, 28]. The GPC is a class I fusion protein located on the virion surface that mediates host cell attachment and pH-dependent membrane fusion; it is the principal target for neutralizing monoclonal antibodies like the Arevirumab cocktail [3, 4, 16, 23]. The NP is the most abundant viral protein, responsible for encapsidating the RNA genome and suppressing the host innate immune response through a C-terminal exonuclease activity that degrades double-stranded RNA [1, 5, 7, 11]. The L protein functions as an RNA-dependent RNA polymerase that drives viral replication and transcription using a 'cap-snatching' mechanism, and it is the target of small-molecule inhibitors such as Ribavirin and Favipiravir [14, 15, 21, 25]. Effective drug development is challenged by the high genetic diversity of LASV lineages and the critical need for early intervention to prevent multi-organ failure and death [2, 24, 27].
Inhibition of viral RNA-dependent RNA polymerase to disrupt genome replication and transcription; Neutralization of the glycoprotein complex to block viral attachment and membrane fusion; Degradation of host capped pre-mRNAs via cap-snatching; Suppression of host innate immune signaling by nucleoprotein-mediated exonuclease activity.
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