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dc.contributor.authorOwen, Danielle Jen
dc.contributor.authorCrump, Colinen
dc.contributor.authorGraham, Stephenen
dc.date.accessioned2015-09-24T11:15:44Z
dc.date.available2015-09-24T11:15:44Z
dc.date.issued2015-09-18en
dc.identifier.citationViruses 2015, 7(9), 5084-5114. doi:10.3390/v7092861en
dc.identifier.issn1999-4915
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/251139
dc.description.abstractAlphaherpesviruses like herpes simplex virus are large DNA viruses characterized by their ability to establish lifelong latent infection in neurons. As for all herpesviruses, alphaherpesvirus virions contain a protein-rich layer called “tegument” that links the DNA-containing capsid to the glycoprotein-studded membrane envelope. Tegument proteins mediate a diverse range of functions during the virus lifecycle, including modulation of the host-cell environment immediately after entry, transport of virus capsids to the nucleus during infection, and wrapping of cytoplasmic capsids with membranes (secondary envelopment) during virion assembly. Eleven tegument proteins that are conserved across alphaherpesviruses have been implicated in the formation of the tegument layer or in secondary envelopment. Tegument is assembled via a dense network of interactions between tegument proteins, with the redundancy of these interactions making it challenging to determine the precise function of any specific tegument protein. However, recent studies have made great headway in defining the interactions between tegument proteins, conserved across alphaherpesviruses, which facilitate tegument assembly and secondary envelopment. We summarize these recent advances and review what remains to be learned about the molecular interactions required to assemble mature alphaherpesvirus virions following the release of capsids from infected cell nuclei.
dc.description.sponsorshipHSV-1 research in the laboratory of CMC is supported by the Leverhulme Trust (Grant RPG-2012-793) and the Biotechnology and Biological Sciences Research Council (Grant BB/M021424/1). SCG is a Sir Henry Dale Fellow jointly funded by the Wellcome Trust and the Royal Society (Grant Number 098406/Z/12/Z)
dc.languageEnglishen
dc.language.isoenen
dc.publisherMDPI
dc.rightsAttribution 2.0 UK: England & Wales*
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/uk/*
dc.subjectvirus egressen
dc.subjectvirus maturationen
dc.subjectherpes simplex virusen
dc.subjectHSV-1en
dc.subjectpseudorabies virusen
dc.subjectPrVen
dc.titleTegument Assembly and Secondary Envelopment of Alphaherpesvirusesen
dc.typeArticle
dc.description.versionThis is the final version of the article. It first appeared from MDPI via http://dx.doi.org/10.3390/v7092861en
prism.endingPage5114
prism.publicationDate2015en
prism.publicationNameVirusesen
prism.startingPage5084
prism.volume7en
dc.rioxxterms.funderBBSRC
dc.rioxxterms.funderWellcome Trust
dc.rioxxterms.projectidBB/M021424/1
dc.rioxxterms.projectid098406/Z/12/Z
dcterms.dateAccepted2015-08-26en
rioxxterms.versionofrecord10.3390/v7092861en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2015-09-18en
dc.contributor.orcidCrump, Colin [0000-0001-9918-9998]
dc.contributor.orcidGraham, Stephen [0000-0003-4547-4034]
dc.identifier.eissn1999-4915
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idWellcome Trust (098406/Z/12/Z)
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/M021424/1)


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Attribution 2.0 UK: England & Wales
Except where otherwise noted, this item's licence is described as Attribution 2.0 UK: England & Wales