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


Milbradt, J; Sonntag, E; Wagner, S; Strojan, H; Wangen, C; Lenac Roviš, Tihana; Lisnić, Berislav; Jonjić, Stipan; Sticht, H; Britt, WJ et al.
Human Cytomegalovirus Nuclear Capsids Associate with the Core Nuclear Egress Complex and the Viral Protein Kinase pUL97. // Viruses-Basel, 10 (2018), 1; 29342872, 21 doi:10.3390/v10010035 (međunarodna recenzija, članak, znanstveni)


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

Autori
Milbradt, J ; Sonntag, E ; Wagner, S ; Strojan, H ; Wangen, C ; Lenac Roviš, Tihana ; Lisnić, Berislav ; Jonjić, Stipan ; Sticht, H ; Britt, WJ ; Schlötzer‐Schrehardt, U ; Marschall, M

Izvornik
Viruses-Basel (1999-4915) 10 (2018), 1; 29342872, 21

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
NEC-capsid interaction ; herpesviral nuclear egress ; human cytomegalovirus ; immunogold-electron microscopy ; nuclear egress complex (NEC) ; viral protein kinase pUL97

Sažetak
The 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

Izvorni jezik
Engleski



POVEZANOST RADA


Projekt / tema
062-0621261-1263 - Molekularni mehanizmi citomegalovirusnog izmicanja imunološkom nadzoru (Stipan Jonjić, )

Ustanove
Medicinski fakultet, Rijeka

Časopis indeksira:


  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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