{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T02:17:16Z","timestamp":1785205036962,"version":"3.55.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1010623","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2022,7,20]],"date-time":"2022-07-20T00:00:00Z","timestamp":1658275200000}}],"reference-count":73,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2022,7,8]],"date-time":"2022-07-08T00:00:00Z","timestamp":1657238400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01GM111795"],"award-info":[{"award-number":["R01GM111795"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI147625"],"award-info":[{"award-number":["R01AI147625"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["K99AI151891"],"award-info":[{"award-number":["K99AI151891"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","award":["55108533"],"award-info":[{"award-number":["55108533"]}],"id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>During replication, herpesviral capsids are translocated from the nucleus into the cytoplasm by an unusual mechanism, termed nuclear egress, that involves capsid budding at the inner nuclear membrane. This process is mediated by the viral nuclear egress complex (NEC) that deforms the membrane around the capsid. Although the NEC is essential for capsid nuclear egress across all three subfamilies of the <jats:italic>Herpesviridae<\/jats:italic>, most studies to date have focused on the NEC homologs from alpha- and beta- but not gammaherpesviruses. Here, we report the crystal structure of the NEC from Epstein-Barr virus (EBV), a prototypical gammaherpesvirus. The structure resembles known structures of NEC homologs yet is conformationally dynamic. We also show that purified, recombinant EBV NEC buds synthetic membranes <jats:italic>in vitro<\/jats:italic> and forms membrane-bound coats of unknown geometry. However, unlike other NEC homologs, EBV NEC forms dimers in the crystals instead of hexamers. The dimeric interfaces observed in the EBV NEC crystals are similar to the hexameric interfaces observed in other NEC homologs. Moreover, mutations engineered to disrupt the dimeric interface reduce budding. Putting together these data, we propose that EBV NEC-mediated budding is driven by oligomerization into membrane-bound coats.<\/jats:p>","DOI":"10.1371\/journal.ppat.1010623","type":"journal-article","created":{"date-parts":[[2022,7,8]],"date-time":"2022-07-08T18:16:50Z","timestamp":1657304210000},"page":"e1010623","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":16,"title":["The nuclear egress complex of Epstein-Barr virus buds membranes through an oligomerization-driven mechanism"],"prefix":"10.1371","volume":"18","author":[{"given":"Michael K.","family":"Thorsen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth B.","family":"Draganova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3113-6958","authenticated-orcid":true,"given":"Ekaterina E.","family":"Heldwein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2022,7,8]]},"reference":[{"key":"ppat.1010623.ref001","volume-title":"Herpesviridae, in Fields Virology","author":"P.E.P.a.B. 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Mettenleiter","year":"2016","journal-title":"Molecular Basis of Herpesvirus Nuclear Egress: the Prototypic Vesicular Nucleo-Cytoplasmic Transport, in Viruses: at the forefront of host interactions"},{"issue":"1","key":"ppat.1010623.ref010","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1146\/annurev-virology-110615-042215","article-title":"Nuclear Exodus: Herpesviruses Lead the Way.","volume":"3","author":"J.M. Bigalke","year":"2016","journal-title":"Annu Rev Virol"},{"key":"ppat.1010623.ref011","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/978-3-319-53168-7_7","article-title":"Herpesvirus Nuclear Egress.","volume":"223","author":"R.J. 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Roller","year":"2010","journal-title":"J Virol"},{"issue":"14","key":"ppat.1010623.ref032","doi-asserted-by":"crossref","first-page":"e00498","DOI":"10.1128\/JVI.00498-19","article-title":"Roles of the Interhexamer Contact Site for Hexagonal Lattice Formation of the Herpes Simplex Virus 1 Nuclear Egress Complex in Viral Primary Envelopment and Replication","volume":"93","author":"J. Arii","year":"2019","journal-title":"Journal of Virology"},{"issue":"21","key":"ppat.1010623.ref033","doi-asserted-by":"crossref","first-page":"12396","DOI":"10.1073\/pnas.1635160100","article-title":"Functional map of human cytomegalovirus AD169 defined by global mutational analysis","volume":"100","author":"D. 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Leigh","year":"2015","journal-title":"Proceedings of the National Academy of Sciences"},{"issue":"23","key":"ppat.1010623.ref038","doi-asserted-by":"crossref","first-page":"2937","DOI":"10.15252\/embj.201592651","article-title":"Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complex","volume":"34","author":"M.F. Lye","year":"2015","journal-title":"Embo j"},{"issue":"46","key":"ppat.1010623.ref039","doi-asserted-by":"crossref","first-page":"27452","DOI":"10.1074\/jbc.C115.686527","article-title":"Crystal Structure of the Human Cytomegalovirus pUL50-pUL53 Core Nuclear Egress Complex Provides Insight into a Unique Assembly Scaffold for Virus-Host Protein Interactions","volume":"290","author":"S.A. 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Gonnella","year":"2005","journal-title":"J Virol"},{"key":"ppat.1010623.ref042","article-title":"High-resolution crystal structures of two prototypical beta- and gamma-herpesviral nuclear egress complexes unravel the determinants of subfamily specificity","author":"Y.A. Muller","year":"2020","journal-title":"J Biol Chem"},{"key":"ppat.1010623.ref043","article-title":"Structural basis for capsid recruitment and coat formation during HSV-1 nuclear egress.","author":"E.B. Draganova","year":"2020","journal-title":"bioRxiv"},{"key":"ppat.1010623.ref044","author":"LLC Schrodinger","year":"2015","journal-title":"The PyMOL Molecular Graphics SystemVersion 1.8."},{"issue":"1","key":"ppat.1010623.ref045","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1002\/pro.3330","article-title":"MolProbity: More and better reference data for improved all-atom structure validation","volume":"27","author":"C.J. 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