{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Prazak V"],"funding":["BMBF grant 05K18BHA","Deutsche Forschungsgemeinschaft","Deutsche Forschungsgemeinschaft (German Research Foundation)","Nuffield Dept of Medicine Prize Studentship","Wellcome Trust"],"pagination":["1842-1855"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7616147"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(7)"],"pubmed_abstract":["The viral nuclear egress complex (NEC) allows herpesvirus capsids to escape from the nucleus without compromising the nuclear envelope integrity. The NEC lattice assembles on the inner nuclear membrane and mediates the budding of nascent nucleocapsids into the perinuclear space and their subsequent release into the cytosol. Its essential role makes it a potent antiviral target, necessitating structural information in the context of a cellular infection. Here we determined structures of NEC-capsid interfaces in situ using electron cryo-tomography, showing a substantial structural heterogeneity. In addition, while the capsid is associated with budding initiation, it is not required for curvature formation. By determining the NEC structure in several conformations, we show that curvature arises from an asymmetric assembly of disordered and hexagonally ordered lattice domains independent of pUL25 or other viral capsid vertex components. Our results advance our understanding of the mechanism of nuclear egress in the context of a living cell."],"journal":["Nature microbiology"],"pubmed_title":["Molecular plasticity of herpesvirus nuclear egress analysed in situ."],"pmcid":["PMC7616147"],"funding_grant_id":["209250","099683","INST 152/ 772-1, 774-1, 775-1, 777-1 FUGG","099683/Z/12/Z","GRK2771 – project no. 453548970","GRK2771 - project no. 453548970","225902","090532","EXC 2155 project no. 390874280","209250/Z/17/Z","225902/Z/22/Z","107806/Z/15/Z","090532/Z/09/Z","107806"],"pubmed_authors":["Bosse JB","Jensen Y","Heumann JM","Klupp BG","Sanders S","Prazak V","Mironova Y","Grunewald K","Vasishtan D","Hagen C","Mettenleiter TC","Grange M","Laugks U"],"additional_accession":[]},"is_claimable":false,"name":"Molecular plasticity of herpesvirus nuclear egress analysed in situ.","description":"The viral nuclear egress complex (NEC) allows herpesvirus capsids to escape from the nucleus without compromising the nuclear envelope integrity. The NEC lattice assembles on the inner nuclear membrane and mediates the budding of nascent nucleocapsids into the perinuclear space and their subsequent release into the cytosol. Its essential role makes it a potent antiviral target, necessitating structural information in the context of a cellular infection. Here we determined structures of NEC-capsid interfaces in situ using electron cryo-tomography, showing a substantial structural heterogeneity. In addition, while the capsid is associated with budding initiation, it is not required for curvature formation. By determining the NEC structure in several conformations, we show that curvature arises from an asymmetric assembly of disordered and hexagonally ordered lattice domains independent of pUL25 or other viral capsid vertex components. Our results advance our understanding of the mechanism of nuclear egress in the context of a living cell.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-01T13:34:55.572Z","creation":"2025-04-04T15:01:52.21Z"},"accession":"S-EPMC7616147","cross_references":{"pubmed":["38918469"],"doi":["10.1038/s41564-024-01716-8"]}}