Vesicular stomatitis virus matrix protein (VSV-M) (VSV-M)

The Vesicular stomatitis virus matrix protein (VSV-M) is a multifunctional structural protein that plays a critical role in the viral life cycle and pathogenesis of the Vesicular stomatitis virus [1]. Structurally, it facilitates the assembly and budding of progeny virions by bridging the viral nucleocapsid with the host-derived lipid envelope [4]. Beyond its structural role, VSV-M is the primary effector of host cell shut-off, where it globally inhibits host transcription and nuclear-cytoplasmic transport of mRNAs [2, 3]. This inhibition is achieved through the formation of a complex with host proteins Rae1 and Nup98, effectively blocking the nuclear pore and preventing the export of antiviral transcripts like interferon-beta [2]. In therapeutic development, VSV-M is a key focus for oncolytic virotherapy; engineered mutations in the M protein, such as the M51R substitution, are used to create viruses that cannot suppress the immune system in healthy cells but remain lethal to cancer cells [5]. While no FDA-approved drugs specifically target VSV-M, it remains a significant target for experimental antiviral compounds, such as cercosporamide and certain flavonoids, designed to restore host immune signaling during infection [3, 6].

Other names

Matrix protein MM proteinVSV-M proteinProtein M

Disruption of the interaction between the viral M protein and the host Rae1-Nup98 complex to restore host nuclear-cytoplasmic transport and innate immune signaling.