Human Cytomegalovirus Nuclear Capsids Associate with the Core Nuclear Egress Complex and the Viral Protein Kinase pUL97

dc.contributor.authorMilbradt, Jens
dc.contributor.authorSonntag, Eric
dc.contributor.authorWagner, Sabrina
dc.contributor.authorStrojan, Hanife
dc.contributor.authorWangen, Christina
dc.contributor.authorRovis, Tihana Lenac
dc.contributor.authorLisnic, Berislav
dc.contributor.authorJonjic, Stipan
dc.contributor.authorSticht, Heinrich
dc.contributor.authorBritt, William J.
dc.contributor.authorSchlötzer-Schrehardt, Ursula
dc.contributor.authorMarschall, Manfred
dc.date.accessioned2019-05-10
dc.date.available2019-04-18
dc.date.created2018
dc.date.issued2019-05-10
dc.description.abstractThe nuclear phase of herpesvirus replication is regulated through the formation of regulatory multi-component protein complexes. Viral genomic replication is followed by nuclear capsid assembly, DNA encapsidation and nuclear egress. The latter has been studied intensely pointing to the formation of a viral core nuclear egress complex (NEC) that recruits a multimeric assembly of viral and cellular factors for the reorganization of the nuclear envelope. To date, the mechanism of the association of human cytomegalovirus (HCMV) capsids with the NEC, which in turn initiates the specific steps of nuclear capsid budding, remains undefined. Here, we provide electron microscopy-based data demonstrating the association of both nuclear capsids and NEC proteins at nuclear lamina budding sites. Specifically, immunogold labelling of the core NEC constituent pUL53 and NEC-associated viral kinase pUL97 suggested an intranuclear NEC-capsid interaction. Staining patterns with phospho-specific lamin A/C antibodies are compatible with earlier postulates of targeted capsid egress at lamina-depleted areas. Important data were provided by co-immunoprecipitation and in vitro kinase analyses using lysates from HCMV-infected cells, nuclear fractions, or infectious virions. Data strongly suggest that nuclear capsids interact with pUL53 and pUL97. Combined, the findings support a refined concept of HCMV nuclear trafficking and NEC-capsid interaction.en
dc.identifier.citationViruses 10.1 (2018). <https://doi.org/10.3390/v10010035>
dc.identifier.doihttps://doi.org/10.3390/v10010035
dc.identifier.opus-id10865
dc.identifier.urihttps://open.fau.de/handle/openfau/10865
dc.identifier.urnurn:nbn:de:bvb:29-opus4-108654
dc.language.isoen
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/deed.de
dc.subjectherpesviral nuclear egress
dc.subjectnuclear egress complex (NEC)
dc.subjectviral protein kinase pUL97
dc.subjectimmunogold-electron microscopy
dc.subjectNEC-capsid interaction
dc.subjecthuman cytomegalovirus
dc.subject.ddcDDC Classification::6 Technik, Medizin, angewandte Wissenschaften :: 61 Medizin und Gesundheit :: 610 Medizin und Gesundheit
dc.titleHuman Cytomegalovirus Nuclear Capsids Associate with the Core Nuclear Egress Complex and the Viral Protein Kinase pUL97en
dc.typearticle
dcterms.publisherFriedrich-Alexander-Universität Erlangen-Nürnberg (FAU)
local.journal.issue1
local.journal.titleViruses
local.journal.volume10
local.sendToDnbfree*
local.subject.fakultaetMedizinische Fakultät
local.subject.sammlungUniversität Erlangen-Nürnberg / Von der FAU geförderte Open Access Artikel / Von der FAU geförderte Open Access Artikel 2018
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