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• W4381952360 abstract "ABSTRACT Nuclear egress is an essential process in herpesviral replication whereby nascent capsids translocate from the nucleus to the cytoplasm. This initial step of nuclear egress – budding at the inner nuclear membrane – is coordinated by the nuclear egress complex (NEC). Composed of the viral proteins UL31 and UL34, NEC deforms the membrane around the capsid as the latter buds into the perinuclear space. NEC oligomerization into a hexagonal membrane-bound lattice is essential for budding because mutations designed to perturb lattice interfaces reduce its budding ability. Previously, we identified an NEC suppressor mutation capable of restoring budding to a mutant with a weakened hexagonal lattice. Here, we show that the suppressor mutation can restore budding to a broad range of budding-deficient NEC mutants thereby acting as a universal suppressor. We demonstrate that the suppressor mutation indirectly promotes the formation of new contacts between the NEC hexamers that, ostensibly, stabilize the hexagonal lattice. This stabilization strategy is powerful enough to override the otherwise deleterious effects of mutations that destabilize the NEC lattice by different mechanisms, resulting in a functional NEC hexagonal lattice and restoration of membrane budding." @default.
• W4381952360 created "2023-06-26" @default.
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• W4381952360 date "2023-06-24" @default.
• W4381952360 modified "2023-09-26" @default.
• W4381952360 title "The universal suppressor mutation in the HSV-1 nuclear egress complex restores membrane budding defects by stabilizing the oligomeric lattice" @default.
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• W4381952360 doi "https://doi.org/10.1101/2023.06.22.546118" @default.
• W4381952360 hasPublicationYear "2023" @default.
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