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Filovirus proteins are the essential molecular components of viruses within the Filoviridae family, most notably Ebola virus (EBOV) and Marburg virus (MARV). These proteins are categorized into structural proteins that form the virion and non-structural proteins that facilitate viral replication and host immune evasion. The glycoprotein (GP) is the primary surface protein responsible for host cell attachment and endosomal entry, making it the target for FDA-approved monoclonal antibodies such as ansuvimab and the REGN-EB3 cocktail (atoltivimab, maftivimab, and odesivimab). The large protein (L) serves as the RNA-dependent RNA polymerase (RdRp) and is the target for small-molecule antivirals like remdesivir and favipiravir, which inhibit viral genome replication. Other critical proteins include the nucleoprotein (NP), which encapsulates the viral RNA, and matrix proteins like VP40 and VP24, which are involved in viral assembly, budding, and the suppression of host interferon signaling. Targeting these proteins is a cornerstone of therapeutic development for treating highly fatal viral hemorrhagic fevers.
Neutralization of viral entry by binding to the glycoprotein (GP) and blocking receptor interaction or membrane fusion; Inhibition of viral RNA synthesis by targeting the RNA-dependent RNA polymerase (L protein) to cause chain termination or lethal mutagenesis; Disruption of viral assembly and budding by targeting matrix proteins (VP40); Inhibition of viral transcription by targeting cofactors like VP30; Blocking of host immune evasion by targeting interferon antagonists (VP35, VP24).
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