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Sudan ebolavirus matrix protein VP40 is the primary structural protein of the Sudan virus (SUDV), a member of the Filoviridae family that causes severe and often fatal hemorrhagic fever [3, 7, 8]. As the most abundantly expressed protein during infection, VP40 is essential for the viral life cycle, coordinating the assembly and budding of new virions at the host cell plasma membrane [4, 11, 13]. It is a multifunctional protein that transitions between different oligomeric states—including dimers, hexamers, and octamers—to regulate distinct processes such as viral transcription, RNA replication, and particle morphogenesis [3, 8, 12]. Beyond its structural role, VP40 contributes to viral pathogenesis by suppressing host innate immune responses and triggering pro-inflammatory signaling through the activation of NF-κB [1, 3, 9]. Because of its critical role in viral egress and its relatively conserved structure, VP40 is considered a high-priority target for the development of novel antiviral drugs, with research focusing on small molecules that disrupt its oligomerization, membrane binding, or interactions with host cellular machinery like the ESCRT complex [4, 6, 14, 17].
Inhibition of viral budding, assembly, and VP40 oligomerization; disruption of membrane binding and host ESCRT complex interactions [4, 6, 12].
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