Adenovirus entry: Stability, uncoating, and nuclear import.
Animals
Humans
Active Transport, Cell Nucleus
Adenoviridae
/ genetics
DNA, Viral
/ genetics
Proteasome Endopeptidase Complex
/ metabolism
Kinesins
COVID-19 Vaccines
COVID-19
Nuclear Pore
/ genetics
Capsid Proteins
/ genetics
Ubiquitin-Protein Ligases
/ metabolism
Nucleoproteins
/ metabolism
Mammals
/ genetics
DNA nuclear transport
Mind bomb 1 (MIB1) E3 ubiquitin ligase
nuclear pore complex (NPC)
ubiquitin proteasome system
virus entry and disassembly
Journal
Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028
Informations de publication
Date de publication:
10 2022
10 2022
Historique:
revised:
09
04
2022
received:
10
03
2022
accepted:
12
04
2022
pubmed:
19
4
2022
medline:
26
10
2022
entrez:
18
4
2022
Statut:
ppublish
Résumé
Adenoviruses (AdVs) are widespread in vertebrates. They infect the respiratory and gastrointestinal tracts, the eyes, heart, liver, and kidney, and are lethal to immunosuppressed people. Mastadenoviruses infecting mammals comprise several hundred different types, and many specifically infect humans. Human adenoviruses are the most widely used vectors in clinical applications, including cancer treatment and COVID-19 vaccination. AdV vectors are physically and genetically stable and generally safe in humans. The particles have an icosahedral coat and a nucleoprotein core with a DNA genome. We describe the concept of AdV cell entry and highlight recent advances in cytoplasmic transport, uncoating, and nuclear import of the viral DNA. We highlight a recently discovered "linchpin" function of the virion protein V ensuring cytoplasmic particle stability, which is relaxed at the nuclear pore complex by cues from the E3 ubiquitin ligase Mind bomb 1 (MIB1) and the proteasome triggering disruption. Capsid disruption by kinesin motor proteins and microtubules exposes the linchpin and renders protein V a target for MIB1 ubiquitination, which dissociates V from viral DNA and enhances DNA nuclear import. These advances uncover mechanisms controlling capsid stability and premature uncoating and provide insight into nuclear transport of nucleic acids.
Identifiants
pubmed: 35434852
doi: 10.1111/mmi.14909
pmc: PMC9790413
doi:
Substances chimiques
DNA, Viral
0
Proteasome Endopeptidase Complex
EC 3.4.25.1
Kinesins
EC 3.6.4.4
COVID-19 Vaccines
0
Capsid Proteins
0
Ubiquitin-Protein Ligases
EC 2.3.2.27
Nucleoproteins
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
309-320Informations de copyright
© 2022 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.
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