Lassa virus matrix protein Z (Z protein) (Z protein)

The Lassa virus matrix protein Z is a small, multifunctional protein essential for the life cycle of the Lassa virus, the causative agent of Lassa fever (UniProt P0C6G1). It plays a central role in viral assembly and budding by interacting with host cell ESCRT (endosomal sorting complex required for transport) machinery, specifically Tsg101 and Alix, through its late domain motifs (PubMed: 12767994). Additionally, the Z protein acts as a negative regulator of viral RNA synthesis by directly interacting with the viral L polymerase, thereby coordinating the transition from replication to assembly (PubMed: 20071563). It also contributes to immune evasion by inhibiting the RIG-I-mediated interferon response, which suppresses the host's innate antiviral defenses (PubMed: 20463082). Structurally, the protein contains a conserved RING finger domain that coordinates two zinc ions, which is critical for its structural integrity and various functions (PubMed: 15140961). Because the Z protein is indispensable for producing infectious progeny and modulating the host environment, it is a high-priority target for antiviral drug development. Current research focuses on identifying small molecules that can disrupt the RING domain or the protein's interactions with host factors to halt viral spread. While no drugs targeting the Z protein are currently FDA-approved, it remains a key focus for therapeutic intervention against Lassa fever.

Other names

Z proteinRING finger protein ZLASV Z proteinMatrix protein ZLASV Z

Inhibition of viral budding by disrupting interactions with host ESCRT machinery or disruption of the RING finger domain to prevent viral assembly and replication regulation.