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Hofmann, S.* ; Stubbe, M.* ; Mai, J.* ; Schreiner, S.

Double-edged role of PML nuclear bodies during human adenovirus infection.

Virus Res. 295:198280 (2021)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
PML nuclear bodies are matrix-bound nuclear structures with a variety of functions in human cells. These nuclear domains are interferon regulated and play an essential role during virus infections involving accumulation of SUMO-dependent host and viral factors. PML-NBs are targeted and subsequently manipulated by adenoviral regulatory proteins, illustrating their crucial role during productive infection and virus-mediated oncogenic transformation. PML-NBs have a longstanding antiviral reputation; however, the genomes of Human Adenoviruses and initial sites of viral transcription/replication are found juxtaposed to these domains, resulting in a double-edged capacity of these nuclear multiprotein/multifunctional complexes. This enigma provides evidence that Human Adenoviruses selectively counteract antiviral responses, and simultaneously benefit from or even depend on proviral PML-NB associated components by active recruitment to PML track-like structures, that are induced during infection. Thereby, a positive microenvironment for adenoviral transcription and replication is created at these nuclear subdomains. Based on the available data, this review aims to provide a detailed overview of the current knowledge of Human Adenovirus crosstalk with nuclear PML body compartments as sites of SUMOylation processes in the host cells, evaluating the currently known principles and molecular mechanisms.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Hadv ; Human Adenovirus ; Pml-nb ; Sumo
ISSN (print) / ISBN 0168-1702
e-ISSN 1872-7492
Journal Virus Research
Quellenangaben Volume: 295, Issue: , Pages: , Article Number: 198280 Supplement: ,
Publisher Elsevier
Publishing Place Radarweg 29, 1043 Nx Amsterdam, Netherlands
Non-patent literature Publications
Reviewing status Peer reviewed
Grants Deutsche Krebshilfe e.V.
Deutsche Forschungsgemeinschaft (DFG German Research Foundation) Germany's Excellence Strategy