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dc.contributor.authorButt, Benjamin G
dc.contributor.authorOwen, Danielle J
dc.contributor.authorJeffries, Cy M
dc.contributor.authorIvanova, Lyudmila
dc.contributor.authorHill, Chris H
dc.contributor.authorHoughton, Jack W
dc.contributor.authorAhmed, Md Firoz
dc.contributor.authorAntrobus, Robin
dc.contributor.authorSvergun, Dmitri I
dc.contributor.authorWelch, John J
dc.contributor.authorCrump, Colin M
dc.contributor.authorGraham, Stephen C
dc.date.accessioned2020-06-12T04:08:25Z
dc.date.available2020-06-12T04:08:25Z
dc.date.issued2020-05-11
dc.date.submitted2019-11-21
dc.identifier.other53789
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/306723
dc.descriptionFunder: Nvidia; FundRef: http://dx.doi.org/10.13039/100007065
dc.descriptionFunder: Wellcome Trust; FundRef: http://dx.doi.org/10.13039/100004440
dc.descriptionFunder: John Lucas Walker Studentship
dc.descriptionFunder: Commonwealth Scholarship Commission; FundRef: http://dx.doi.org/10.13039/501100000867
dc.description.abstractHerpesviruses acquire their membrane envelopes in the cytoplasm of infected cells via a molecular mechanism that remains unclear. Herpes simplex virus (HSV)−1 proteins pUL7 and pUL51 form a complex required for efficient virus envelopment. We show that interaction between homologues of pUL7 and pUL51 is conserved across human herpesviruses, as is their association with trans-Golgi membranes. We characterized the HSV-1 pUL7:pUL51 complex by solution scattering and chemical crosslinking, revealing a 1:2 complex that can form higher-order oligomers in solution, and we solved the crystal structure of the core pUL7:pUL51 heterodimer. While pUL7 adopts a previously-unseen compact fold, the helix-turn-helix conformation of pUL51 resembles the cellular endosomal complex required for transport (ESCRT)-III component CHMP4B and pUL51 forms ESCRT-III–like filaments, suggesting a direct role for pUL51 in promoting membrane scission during virus assembly. Our results provide a structural framework for understanding the role of the conserved pUL7:pUL51 complex in herpesvirus assembly.
dc.languageen
dc.publishereLife Sciences Publications, Ltd
dc.rightsAttribution 4.0 International (CC BY 4.0)en
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectResearch Article
dc.subjectMicrobiology and Infectious Disease
dc.subjectStructural Biology and Molecular Biophysics
dc.subjectsmall-angle X-ray scattering (SAXS)
dc.subjectsecondary envelopment
dc.subjectvirus budding
dc.subjectfocal adhesions
dc.subjecthuman cytomegalovirus (hcmv)
dc.subjectVirus
dc.titleInsights into herpesvirus assembly from the structure of the pUL7:pUL51 complex
dc.typeArticle
dc.date.updated2020-06-12T04:08:24Z
prism.publicationNameeLife
prism.volume9
dc.identifier.doi10.17863/CAM.53811
dcterms.dateAccepted2020-05-07
rioxxterms.versionofrecord10.7554/elife.53789
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
datacite.contributor.supervisoreditor: Sundquist, Wesley I
datacite.contributor.supervisorsenior_editor: Wolberger, Cynthia
dc.contributor.orcidButt, Benjamin G [0000-0001-6718-0470]
dc.contributor.orcidHill, Chris H [0000-0001-7037-0611]
dc.contributor.orcidCrump, Colin M [0000-0001-9918-9998]
dc.contributor.orcidGraham, Stephen C [0000-0003-4547-4034]
dc.identifier.eissn2050-084X
pubs.funder-project-idWellcome (098406/Z/12/B)
pubs.funder-project-idRoyal Society (098406/Z/12/B)
datacite.issupplementedby.urlhttps://doi.org/10.17863/CAM.44914


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Attribution 4.0 International (CC BY 4.0)
Except where otherwise noted, this item's licence is described as Attribution 4.0 International (CC BY 4.0)