Marburgvirus VP24 protein (VP24)

The Marburgvirus VP24 protein is a structural viral protein that functions as a minor matrix protein in the filovirus life cycle, distinct from its Ebola virus counterpart. It associates with lipid membranes peripherally, oligomerizes into tetramers or higher-order structures, and interacts with the nucleoprotein NP to facilitate nucleocapsid assembly and transport to budding sites at the plasma membrane. VP24 is recruited into virus-like particles induced by the major matrix protein VP40 but does not alter their morphology or budding efficiency; however, silencing VP24 expression significantly impairs infectious particle release without affecting viral transcription or replication. Its crystal structure reveals a pyramid-shaped α/β domain with conserved pockets, a projecting β-shelf, and a flexible N-terminal strand, differing from ebolavirus VP24 in lacking immunosuppressive activity. In Marburg virus infection, VP24 binds human Keap1 via K-loop cysteine residues, promoting Nrf2 nuclear accumulation and cytoprotective antioxidant responses that support viral propagation. As a critical component of the viral matrix between the nucleocapsid and envelope, VP24 is essential for forming transport-compete nt nucleocapsids and enabling progeny virion production, positioning it as a potential antiviral target despite limited approved drugs.

Other names

MARV VP24mVP24