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The Taï Forest virus nucleoprotein (NP) is a primary structural protein of the Taï Forest virus (TAFV), a member of the Ebolavirus genus [1, 3]. Its main function is the encapsidation of the viral negative-sense RNA genome, forming a helical nucleocapsid that protects the genetic material from host cell nucleases and the innate immune response [1, 2]. NP is essential for viral replication and transcription, acting as a template for the viral polymerase complex and recruiting host cell phosphatases, such as PP2A, to regulate the activity of the transcription factor VP30 [2, 4]. It also facilitates the assembly of the nucleocapsid through interactions with other viral proteins like VP35 and VP40 [1, 4]. In clinical applications, NP is a major target for diagnostic tools, including rapid antigen tests and ELISA, due to its high abundance in infected cells and virions [2, 5]. Furthermore, it is utilized as a key antigen in multivalent vaccine candidates, such as MVA-BN-Filo (Mvabea), to stimulate robust T-cell and B-cell immune responses [5, 6]. Research into direct-acting antivirals often targets the conserved protein-protein interaction interfaces of NP to disrupt the viral life cycle [2, 7]. Although TAFV has caused fewer human cases than other ebolaviruses, NP remains a critical focus for pan-ebolavirus therapeutic and preventive strategies [3, 6].
Vaccine antigen for inducing humoral and cellular immune responses; inhibition of viral replication and transcription via disruption of protein-protein interactions (e.g., NP-VP35 or NP-PP2A interfaces)
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