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dc.contributor.authorAlbecka, Anna
dc.contributor.authorLaine, Romain F
dc.contributor.authorJanssen, Anne FJ
dc.contributor.authorKaminski, Clemens F
dc.contributor.authorCrump, Colin M
dc.date.accessioned2015-09-25T11:51:35Z
dc.date.available2015-09-25T11:51:35Z
dc.date.issued2016-01
dc.identifier.citationTraffic 2015, 17(1): 21–39. doi:10.1111/tra.12340
dc.identifier.issn1398-9219
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/251157
dc.description.abstractHerpes simplex virus-1 (HSV-1) is a large enveloped DNA virus that belongs to the family of Herpesviridae. It has been recently shown that the cytoplasmic membranes that wrap the newly assembled capsids are endocytic compartments derived from the plasma membrane. Here, we show that dynamin-dependent endocytosis plays a major role in this process. Dominant-negative dynamin and clathrin adaptor AP180 significantly decrease virus production. Moreover, inhibitors targeting dynamin and clathrin lead to a decreased transport of glycoproteins to cytoplasmic capsids, confirming that glycoproteins are delivered to assembly sites via endocytosis. We also show that certain combinations of glycoproteins colocalize with each other and with the components of clathrin-dependent and -independent endocytosis pathways. Importantly, we demonstrate that the uptake of neutralizing antibodies that bind to glycoproteins when they become exposed on the cell surface during virus particle assembly leads to the production of non-infectious HSV-1. Our results demonstrate that transport of viral glycoproteins to the plasma membrane prior to endocytosis is the major route by which these proteins are localized to the cytoplasmic virus assembly compartments. This highlights the importance of endocytosis as a major protein-sorting event during HSV-1 envelopment.
dc.description.sponsorshipThis work was supported by grants from the Leverhulme Trust (grant RPG‐2012‐793), the Royal Society (University Research Fellowship UF090010), the Engineering and Physical Sciences Research Council, UK (grant EP/H018301/1, EP/L015889/1) and by the Medical Research Council (grant MR/K015850/1).
dc.languageeng
dc.language.isoen
dc.publisherWiley
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectHSV
dc.subjectdSTORM
dc.subjectdynamin
dc.subjectendocytosis
dc.subjectglycoprotein
dc.subjectvirus assembly
dc.subjectAnimals
dc.subjectCOS Cells
dc.subjectCercopithecus aethiops
dc.subjectClathrin
dc.subjectDynamins
dc.subjectEndocytosis
dc.subjectGlycoproteins
dc.subjectHerpesvirus 1, Human
dc.subjectHumans
dc.subjectMonomeric Clathrin Assembly Proteins
dc.subjectProtein Transport
dc.subjectVero Cells
dc.subjectViral Proteins
dc.subjectVirus Assembly
dc.titleHSV-1 Glycoproteins Are Delivered to Virus Assembly Sites Through Dynamin-Dependent Endocytosis.
dc.title.alternativeHSV-1 glycoprotein endocytosis
dc.typeArticle
prism.endingPage39
prism.issueIdentifier1
prism.publicationNameTraffic
prism.startingPage21
prism.volume17
dc.rioxxterms.funderEPSRC
dc.rioxxterms.funderMRC
dc.rioxxterms.projectidEP/H018301/1
dc.rioxxterms.projectidEP/L015889/1
dc.rioxxterms.projectidMR/K015850/1
dcterms.dateAccepted2015-10-07
rioxxterms.versionofrecord10.1111/tra.12340
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
rioxxterms.licenseref.startdate2015-10-07
dc.contributor.orcidKaminski, Clemens [0000-0002-5194-0962]
dc.contributor.orcidCrump, Colin [0000-0001-9918-9998]
dc.identifier.eissn1600-0854
rioxxterms.typeJournal Article/Review
pubs.funder-project-idLeverhulme Trust (RPG-2012-793)
pubs.funder-project-idEngineering and Physical Sciences Research Council (EP/H018301/1)
pubs.funder-project-idMedical Research Council (MR/K015850/1)
pubs.funder-project-idEngineering and Physical Sciences Research Council (EP/L015889/1)
cam.issuedOnline2015-10-13
cam.orpheus.successThu Jan 30 12:55:40 GMT 2020 - The item has an open VoR version.
rioxxterms.freetoread.startdate2100-01-01


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