The Marburg virus (MARV) is an enveloped, single-stranded negative-sense RNA virus belonging to the genus Marburgvirus within the family Filoviridae. This virus is closely related to the Ebola virus, both being highly pathogenic pathogens. The natural host of MARV is believed to be African fruit bats, and the virus can be transmitted through contact with infected animals or their bodily fluids. The World Health Organization (WHO) has classified it as one of the highest-priority pathogens. Given its potential public health risks, continuous monitoring and fundamental research are crucial for enhancing preparedness and understanding its biological characteristics.

The Marburg virus belongs to the family Filoviridae, and its viral particles exhibit diverse morphologies, often appearing as long filaments, rods, or branched structures, with lengths typically ranging from 800 to 14,000 nm and a diameter of approximately 80 nm. The viral genome is a non-segmented single-stranded negative-sense RNA, approximately 19 kb in size, encoding seven structural proteins, including the nucleoprotein (NP), viral proteins VP35, VP40, glycoprotein (GP), VP30, VP24, and the RNA-dependent RNA polymerase (L protein). The entire viral particle is structured from the inside out, primarily comprising the ribonucleoprotein complex (RNP), the matrix layer, and the viral envelope. The RNP contains the genomic RNA tightly bound to NP, VP35, VP30, and L proteins, forming the core for viral transcription and replication. The matrix layer consists of VP40 and VP24 proteins. VP40 is the major matrix protein and plays a central role in viral particle assembly, budding, and maintaining morphology, while VP24 is involved in nucleocapsid assembly and host immune modulation. The viral envelope is derived from the host cell membrane and is regularly embedded with spikes formed by viral glycoprotein (GP) trimers. GP is responsible for recognizing host cell surface receptors, mediating the fusion of the viral envelope with the host cell membrane, and facilitating cellular entry, making it a key molecule for viral infection. At the same time, GP is also the primary antigen that stimulates the host to produce specific neutralizing antibodies. This characteristic makes it an important target for the development of serological detection methods, vaccine design, and therapeutic antibody research.

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