Molecular mechanisms underlying assembly and release of Lassa virus

Lassa virus, an Old World member of the family Arenaviridae, is a rodent-borne RNA virus of African origin that can cause lethal hemorrhagic fever as a severe clinical manifestation in humans. Its bi-segmented RNA genome encodes four polypeptides: the nucleoprotein NP, the surface glycoprotein GP, the polymerase L, and the small RING finger protein Z, which is the functional counterpart of the matrix proteins found in other negative-stranded enveloped RNA viruses.
Like other arenaviruses, Lassa virus exits its host cells by budding from the plasma membrane. The Z protein plays a key role in this process. On the one hand, the Z protein mediates all of the essential virion assembly events that ensure the packaging of all viral components required for infectivity, while on the other hand, Z protein alone facilitates virus-host protein-protein interactions that are necessary but also sufficient to create viral particles. In my presentation I will present our current understanding of the virus-virus-protein interactions as well as virus-host protein-protein interactions, which are necessary for the assembly and release of infectious Lassa virions.