When resources are exhausted, the cell lyses, releasing a final burst of virus. Capsid protein size variants VP1 and VP2 are synthesized in an approximately 5:1 ratio in the cytoplasm. NS2:CRM1 interactions mediate virion exit from the nucleus. Virions are internalized in CopII vesicles in the endoplasmic reticulum and modified as they are trafficked through the Golgi to the cell surface for early release, while the cell continues to amplify viral DNA. VP2 N termini are extruded at the virion surface as DNA is encapsidated, carrying nuclear export signals. VP2 homotrimers and VP1+(VP2)2 heterotrimers assemble in cytoplasm, creating a structure-dependent, nonconventional nuclear localization motif. Trimers are transported into the nucleus, where they assemble into empty capsids. The nucleolus is implicated as assembly site for AAVs, but not apparently for MVM. The single DNA strand is packaged 3'-to-5' into the preformed capsid via a fivefold pore, driven by the viral SF3 helicase. Viral DNA is amplified by unidirectional displacement synthesis through duplex intermediates. NS1 excises unit-length genomes and is left covalently attached to all 5' ends (purple circles). The release of displaced progeny strands is concomitant with packaging. Click on each number for an explanation of the corresponding step; click on “X” to close explanation box Use “ESC” key to exit