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- W2585722476 abstract "Herpesviruses are unusual among enveloped viruses because they bud twice yet acquire a single envelope. They are also the only known mammalian viruses that bud into the nuclear envelope. Recently, we discovered that the herpesvirus nuclear egress complex (NEC) could bud membranes without the help of other proteins and that it formed a coat-like hexagonal scaffold inside the budding membrane. This discovery established the NEC as the first virally encoded budding machine that operates at the nuclear, as opposed to cytoplasmic, membrane but left unknown the structure of the NEC coat and its role in the budding process. To bridge this gap in our knowledge, we determined the 2.8-A crystal structure of the NEC from Herpes Simplex virus (HSV). In crystals, NEC packs into a hexagonal lattice that mimics the hexagonal NEC coats within budded vesicles. The crystal structure of the NEC lattice thus reveals molecular interactions that generate the hexagonal coat. To determine the role of the hexagonal NEC lattice in budding, we mutated residues at the oligomeric interfaces observed in the crystals with mutagenesis. Perturbation of the oligomeric interfaces through mutagenesis blocked NEC-mediated budding in vitro confirming that formation of the hexagonal NEC lattice drives budding. The NEC structure provide a three-dimensional blueprint for further dissection of its unique budding mechanism. Moreover, the structure represents the first atomic-level view of an oligomeric array formed by a membrane-deforming protein." @default.
- W2585722476 created "2017-02-10" @default.
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- W2585722476 date "2017-02-01" @default.
- W2585722476 modified "2023-09-29" @default.
- W2585722476 title "The Great Nuclear Escape: Structure-Based Mechanism of Membrane Budding during Nuclear Egress of Herpesviruses" @default.
- W2585722476 doi "https://doi.org/10.1016/j.bpj.2016.11.222" @default.
- W2585722476 hasPublicationYear "2017" @default.
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