Chromatin organization regulates viral egress dynamics
Aho, V., Myllys, M., Ruokolainen, V., Hakanen, S., Mäntylä, E., Virtanen, J., Hukkanen, V., Kühn, T., Timonen, J., Mattila, K., Larabell, C. A., & Vihinen-Ranta, M. (2017). Chromatin organization regulates viral egress dynamics. Scientific Reports, 7, Article 3692. https://doi.org/10.1038/s41598-017-03630-y
Published in
Scientific ReportsAuthors
Date
2017Discipline
Solu- ja molekyylibiologiaFysiikkaNanoscience CenterCell and Molecular BiologyPhysicsNanoscience CenterCopyright
© the Authors, 2017. This article is licensed under a Creative Commons Attribution 4.0 International License.
Various types of DNA viruses are known to elicit the formation of a large nuclear viral replication
compartment and marginalization of the cell chromatin. We used three-dimensional soft x-ray
tomography, confocal and electron microscopy, combined with numerical modelling of capsid diffusion
to analyse the molecular organization of chromatin in herpes simplex virus 1 infection and its effect
on the transport of progeny viral capsids to the nuclear envelope. Our data showed that the formation
of the viral replication compartment at late infection resulted in the enrichment of heterochromatin
in the nuclear periphery accompanied by the compaction of chromatin. Random walk modelling of
herpes simplex virus 1–sized particles in a three-dimensional soft x-ray tomography reconstruction of
an infected cell nucleus demonstrated that the peripheral, compacted chromatin restricts viral capsid
diffusion, but due to interchromatin channels capsids are able to reach the nuclear envelope, the site of
their nuclear egress.
...


Publisher
Nature Publishing GroupISSN Search the Publication Forum
2045-2322Keywords
Original source
https://www.nature.com/articles/s41598-017-03630-y.pdfPublication in research information system
https://converis.jyu.fi/converis/portal/detail/Publication/27074248
Metadata
Show full item recordCollections
License
Except where otherwise noted, this item's license is described as © the Authors, 2017. This article is licensed under a Creative Commons Attribution 4.0 International License.
Related items
Showing items with similar title or keywords.
-
Herpes simplex virus 1 induces egress channels through marginalized host chromatin
Myllys, Markko; Ruokolainen, Visa; Aho, Vesa; Smith, Elizabeth A.; Hakanen, Satu; Peri, Piritta; Salvetti, Anna; Timonen, Jussi; Hukkanen, Veijo; Larabell, Carolyn A.; Vihinen-Ranta, Maija (Nature Publishing Group, 2016)Lytic infection with herpes simplex virus type 1 (HSV-1) induces profound modification of the cell nucleus including formation of a viral replication compartment and chromatin marginalization into the nuclear periphery. ... -
The role of cellular cytoskeleton in the egress of Coxsackievirus B3
Niva, Juho (2020)Enterovirus-sukuun kuuluva Coxsackievirus B3 aiheuttaa vakavia sairauksia mm. sydänlihastulehdusta, kardiomyopatiaa ja tyypin 1 diabetesta. CVB3 on yksijuosteita RNA:ta sisältävä virus, joka replikoituu solun sytoplasmassa. ... -
PKR phosphorylation as an Indicator for echovirus 1 genome egress from endosomes
Aspelin, William (2019)Isäntäsolut ovat kehittäneet useita keinoja tunnistaa viruksia ja estää niiden lisääntyminen. Yksi näistä keinoista on translaatioon vaadittavan tukiproteiini eukaryotic intiation factor 2:n (eIF2) fosforylaatio, joka estää ... -
Virus-host interactions during nuclear egress of parvoviruses
Mattola, Salla (2022)Autonomic parvoviruses, small non-enveloped ssDNA viruses, encode only a limited number of proteins, which makes them highly dependent on the functions provided by the host cell. Besides two capsid proteins, VP1 and VP2, ... -
Nuclear entry and egress of parvoviruses
Mattola, Salla; Aho, Vesa; Bustamante‐Jaramillo, Luisa F.; Pizzioli, Edoardo; Kann, Michael; Vihinen‐Ranta, Maija (Wiley, 2022)Parvoviruses are small non-enveloped single-stranded DNA viruses, which depend on host cell nuclear transcriptional and replication machinery. After endosomal exposure of nuclear localization sequence and a phospholipase ...