(1) VP40 is synthesized and exists primarily as a dimer at very low protein concentrations that is mediated by alpha-helical NTD interactions. Mutation of residues in the dimer interface will significantly impair VP40 dimerization as well as its localization to the plasma membrane. (2) VP40 dimers are able to rearrange into an octameric form that is triggered by RNA binding [12]. The ring octamer is formed through an oligomerization interface in the NTD that is distinct from the N-terminal alpha-helical dimer interface. (3) VP40 dimers are trafficked to the plasma membrane and hijack the COPII vesicle protein, Sec24C for this process. VP40 also undergoes a number of post-translational modifications that are important for protein stability and viral budding including SUMOylation, ubiquitylation and phosphorylation. (4) Additionally, VP40 moves at the plasma membrane in a ballistic motion that is dependent on actin polymerization. Actin also plays an important role in increasing virus egress. (5) At the plasma membrane inner leaflet, VP40 binds PS and PI(4,5)P₂ and can assemble into (6) oligomers via CTD–CTD interactions. VP40 oligomerization and formation of the virus matrix layer is an essential step in proper virion or VLP formation. (7) As VP40 oligomerization occurs, PS can be detected on the outer plasma membrane leaflet and exposed PS plays an important role in viral attachment and entry through host receptor interactions. (8) As formation of VP40 assembly and virus budding sites ensues, the virus nucleocapsid is recruited to sites of assembly through an actin-dependent mechanism. (9) A number of different host factors interact with VP40 at or near the plasma membrane including Tsg101, NEDD4, IQGAP1 and Amot. These interactions help facilitate the late stages of virus budding and membrane scission. (10) Mature virions or VLPs are released from host cell membrane giving rise to filamentous particles. Created with BioRender.com.