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Molecular plasticity of herpesvirus nuclear egress analysed in situ.
Prazák, Vojtech; Mironova, Yuliia; Vasishtan, Daven; Hagen, Christoph; Laugks, Ulrike; Jensen, Yannick; Sanders, Saskia; Heumann, John M; Bosse, Jens B; Klupp, Barbara G; Mettenleiter, Thomas C; Grange, Michael; Grünewald, Kay.
Afiliación
  • Prazák V; Centre for Structural Systems Biology, Hamburg, Germany.
  • Mironova Y; Leibniz Institute of Virology, Hamburg, Germany.
  • Vasishtan D; Oxford Particle Imaging Centre, Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.
  • Hagen C; Department of Biochemistry, University of Oxford, Oxford, UK.
  • Laugks U; Centre for Structural Systems Biology, Hamburg, Germany.
  • Jensen Y; Leibniz Institute of Virology, Hamburg, Germany.
  • Sanders S; Department of Chemistry, University of Hamburg, Hamburg, Germany.
  • Heumann JM; Centre for Structural Systems Biology, Hamburg, Germany.
  • Bosse JB; Leibniz Institute of Virology, Hamburg, Germany.
  • Klupp BG; Oxford Particle Imaging Centre, Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.
  • Mettenleiter TC; Department of Biochemistry, University of Oxford, Oxford, UK.
  • Grange M; Centre for Structural Systems Biology, Hamburg, Germany.
  • Grünewald K; Leibniz Institute of Virology, Hamburg, Germany.
Nat Microbiol ; 9(7): 1842-1855, 2024 Jul.
Article en En | MEDLINE | ID: mdl-38918469
ABSTRACT
The viral nuclear egress complex (NEC) allows herpesvirus capsids to escape from the nucleus without compromising the nuclear envelope integrity. The NEC lattice assembles on the inner nuclear membrane and mediates the budding of nascent nucleocapsids into the perinuclear space and their subsequent release into the cytosol. Its essential role makes it a potent antiviral target, necessitating structural information in the context of a cellular infection. Here we determined structures of NEC-capsid interfaces in situ using electron cryo-tomography, showing a substantial structural heterogeneity. In addition, while the capsid is associated with budding initiation, it is not required for curvature formation. By determining the NEC structure in several conformations, we show that curvature arises from an asymmetric assembly of disordered and hexagonally ordered lattice domains independent of pUL25 or other viral capsid vertex components. Our results advance our understanding of the mechanism of nuclear egress in the context of a living cell.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Núcleo Celular / Cápside / Microscopía por Crioelectrón / Liberación del Virus / Membrana Nuclear Límite: Humans Idioma: En Revista: Nat Microbiol Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Núcleo Celular / Cápside / Microscopía por Crioelectrón / Liberación del Virus / Membrana Nuclear Límite: Humans Idioma: En Revista: Nat Microbiol Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido