Matrix protein of vesicular stomatitis virus (M protein)

The matrix protein of vesicular stomatitis virus (commonly abbreviated as M protein) is a major structural protein located between the viral lipid envelope and the ribonucleoprotein core[1][4][5][8]. It plays essential roles in the later phases of the viral life cycle by: - Facilitating virus assembly and budding at the host cell membrane by bridging the nucleocapsid and envelope[2][3][4][5][8]. - Inhibiting host gene expression through the blockade of mRNA nuclear export, primarily via direct interaction with the Rae1-Nup98 complex, which suppresses interferon signaling and establishment of an antiviral state in infected cells[1][7]. - Inducing apoptosis and cytopathic effects, such as cell rounding and cytoskeleton disorganization, by activating apoptotic pathways and interfering with cellular processes[1]. Structurally, the M protein adopts a unique fold with a central globular domain and flexible regions important for self-assembly and membrane binding[1][5]. There is strong evidence that the M protein is the principal viral factor causing the shutdown of host macromolecular synthesis in VSV-infected cells[1][5][7]. It is fundamental for the viral life cycle, making it a potential target in antiviral strategies and for modifying viral vectors, though direct-acting drugs targeting this protein are not currently established.

Other names

vesiculovirus matrix proteinVSV M proteinVSIV matrix protein

Inhibits host gene expression (by blocking mRNA export via interaction with Rae1-Nup98 complex); Promotes virion assembly by bridging viral nucleocapsid and membrane; Induces apoptosis in infected cells.