Sudan ebolavirus matrix protein VP40 (SUDV VP40) (SUDV VP40)

Sudan ebolavirus matrix protein VP40 is the primary structural component of the Sudan virus (SUDV) and is indispensable for the viral life cycle [2, 4]. It orchestrates the assembly and budding of new virions from the plasma membrane of infected host cells by interacting with host proteins such as TSG101 and NEDD4 via its late-domain motifs [5, 6]. VP40 is unique in its ability to adopt multiple conformational states—including dimers, hexamers, and octamers—each serving distinct roles such as structural formation, membrane binding, and regulation of viral transcription [2, 4]. Beyond its structural role, SUDV VP40 contributes to pathogenesis by suppressing host RNA interference (RNAi) and triggering pro-inflammatory responses through the activation of the NF-κB pathway [3, 6]. As a critical factor in viral egress and host immune evasion, it is a major target for the development of antiviral therapeutics, including small-molecule inhibitors and antisense oligonucleotides [1, 12]. Current drug discovery efforts focus on disrupting its oligomerization or its recruitment to the plasma membrane to halt the production of infectious progeny [8, 12]. Experimental compounds like sangivamycin have shown promise in inhibiting VP40-mediated assembly, while repositioned drugs like nilotinib may affect its function through phosphorylation pathways [1, 12]. Understanding the high-resolution structure of the SUDV VP40 dimer is essential for designing species-specific or pan-ebolavirus medical countermeasures [4, 8].

Other names

Matrix protein VP40SUDV VP40VP40Matrix protein

Inhibition of viral assembly and budding by disrupting VP40 oligomerization, membrane binding, or interaction with host ESCRT machinery.