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Marburg virus antigens refer to the set of seven structural proteins encoded by the Marburg virus (MARV), a highly pathogenic member of the Filoviridae family and the causative agent of Marburg virus disease. The surface glycoprotein (GP) is the primary therapeutic target for neutralizing antibodies and vaccines, as it mediates viral attachment, fusion, and entry into host cells by binding to the Niemann-Pick C1 receptor [1, 10]. Inside the virion, the nucleoprotein (NP) and the large (L) protein form the nucleocapsid complex essential for viral RNA replication and transcription [14, 15]. Other critical antigens include the matrix proteins VP40 and VP24, along with the polymerase cofactor VP35, which facilitate viral assembly and the evasion of host innate immune responses by inhibiting interferon signaling [10, 18]. Current therapeutic development focuses on monoclonal antibodies that target the GP to block entry and small-molecule polymerase inhibitors targeting the L protein, alongside various vaccine candidates designed to provide long-term immunity [5, 7, 16, 23].
Monoclonal antibodies such as MR191 neutralize the virus by binding to the glycoprotein (GP) and blocking its interaction with the host receptor Niemann-Pick C1 (NPC1) [1, 4]. Nucleoside analogs including remdesivir and galidesivir act by inhibiting the RNA-dependent RNA polymerase (L protein), leading to premature termination of viral RNA replication and transcription [6, 7]. Vaccines utilize viral vectors or genetic material to express viral antigens, primarily the GP, to prime the host immune system and generate protective neutralizing antibodies and T-cell responses [8, 13, 16].
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