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dc.contributor.authorClarke, Richard W.
dc.date.accessioned2016-08-24T14:48:26Z
dc.date.available2016-08-24T14:48:26Z
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/257402
dc.descriptionThe main file shows a superstructure the paper proposes for HSV's entry-essential glycoproteins that would stabilize a compact form of the gB fusogen: The compact form of the gB trimer (blue/mauve/cyan) is surrounded by a ring of three gHgL heterodimers (pink/grey/magenta) that are in turn held in place by three gD glycoproteins (green). Also shown are Nectin (orange) and HVEM (purple) in their binding configurations to gD, illustrating the lack of steric hindrance with the rest of the superstructure. These are held to be transition states, because either Nectin or HVEM can displace a region on gD that then binds to gHgL, which would cause each one in turn to adopt the open configuration shown in the other file. Once all three gHgL are in the open configuration the hairpin loops of gB would be free to rotate, allowing gB to spring upwards into the cell membrane. Active cellular forces pulling inwards on the gD receptors then continue to pull the entire complex via gD, causing fusion of the cell membrane with the viral envelope and releasing the tegument and capsid into the cell. This mechanism is consistent with the finding [JACS 2013, 135, 11175 dx.doi.org/10.1021/ja4038406 ] that a single gD unbound by antibody is sufficient for HSV entry to some cell types, because each superstructure would require all three gDs to be activated by binding one of their receptors, Nectin-1 or Nectin-2, Herpes Virus Entry Mediator (HVEM), or 3-O-Sulfated Heparan Sulfate (3OSHS) on Syndecan-1 or Syndecan-2. For full references please see ACS Infectious Diseases, 1.9 (2015): 403-415 http://pubs.acs.org/doi/abs/10.1021/acsinfecdis.5b00059 Open Access: https://www.repository.cam.ac.uk/handle/1810/257391en
dc.description.sponsorshipChrist's College, University of Cambridge [JRF]en
dc.formatUCSF Chimeraen
dc.publisherUniversity of Cambridgeen
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectentry mechanismen
dc.subjectHerpes Simplex Virusen
dc.subjectglycoproteinsen
dc.subjectstructureen
dc.subjectgBen
dc.subjectgHgLen
dc.subjectgDen
dc.subjectNectinen
dc.subjectHVEMen
dc.subject3OSHSen
dc.subjectSyndecanen
dc.titleResearch data supporting “Forces and Structures of the Herpes Simplex Virus (HSV) Entry Mechanism”en
dc.typeDataseten
dc.identifier.doi10.17863/CAM.1635
pubs.declined2017-10-11T13:54:41.964+0100
datacite.iscitedby.urlhttps://www.repository.cam.ac.uk/handle/1810/257391en
dcterms.formatzip, pyen
cam.relation.otherpublicationhttp://dx.doi.org/10.1021/ja4038406
cam.relation.otherpublicationhttp://dx.doi.org/10.1529/biophysj.107.106351
datacite.issupplementto.doi10.1021/acsinfecdis.5b00059


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