ArticleJournal of virology2001
Functional analysis of adenovirus protein IX identifies domains involved in capsid stability, transcriptional activity, and nuclear reorganization.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Understanding the performance of HIV-1 viral vector vaccines: adenovirus and poxvirus case studies.Frontiers in immunology · 2025Review
- Understanding the Neurotrophic Virus Mechanisms and Their Potential Effect on Systemic Lupus Erythematosus Development.Brain sciences · 2024Review
- Article
- Near-atomic structure of an atadenovirus reveals a conserved capsid-binding motif and intergenera variations in cementing proteins.Science advances · 2021Article
- Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins.Viruses · 2020Review
- Fusion of Large Polypeptides to Human Adenovirus Type 5 Capsid Protein IX Can Compromise Virion Stability and DNA Packaging Capacity.Journal of virology · 2020Article
- Fluorescent protein tagging of adenoviral proteins pV and pIX reveals 'late virion accumulation compartment'.PLoS pathogens · 2020Article
- Nup358 and Transportin 1 Cooperate in Adenoviral Genome Import.Journal of virology · 2020Article
- Review
- The Role of Hexon Protein as a Molecular Mold in Patterning the Protein IX Organization in Human Adenoviruses.Journal of molecular biology · 2017Article
- Bovine adenovirus type 3 virions cannot be rescuedJournal of veterinary science · 2017Article
- Cryo-EM structure of human adenovirus D26 reveals the conservation of structural organization among human adenoviruses.Science advances · 2017Article
- Article
- Design stars: how small DNA viruses remodel the host nucleus.Future virology · 2012Article
- Adenovirus sequesters phosphorylated STAT1 at viral replication centers and inhibits STAT dephosphorylation.Journal of virology · 2011Article
- Genetic incorporation of human metallothionein into the adenovirus protein IX for non-invasive SPECT imaging.PloS one · 2011Article
- A cytoplasmic negative regulator isoform of ATF7 impairs ATF7 and ATF2 phosphorylation and transcriptional activity.PloS one · 2011Article
- Identification of a previously unrecognized promoter that drives expression of the UXP transcription unit in the human adenovirus type 5 genome.Journal of virology · 2010Article
- Article
- Retargeting of adenovirus vectors through genetic fusion of a single-chain or single-domain antibody to capsid protein IX.Journal of virology · 2010Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The product of adenovirus (Ad) type 5 gene IX (pIX) is known to actively participate in the stability of the viral icosahedron, acting as a capsid cement. We have previously demonstrated that pIX is also a transcriptional activator of several viral and cellular TATA-containing promoters, likely contributing to the transactivation of the Ad expression program. By extensive mutagenesis, we have now delineated the functional domains involved in each of the pIX properties: residues 22 to 26 of the highly conserved N-terminal domain are crucial for incorporation of the protein into the virion; specific residues of the C-terminal leucine repeat are responsible for pIX interactions with itself and possibly other proteins, a property that is critical for pIX transcriptional activity. We also show that pIX takes part in the virus-induced nuclear reorganization of late infected cells: the protein induces, most likely through self-assembly, the formation of specific nuclear structures which appear as dispersed nuclear globules by immunofluorescence staining and as clear amorphous spherical inclusions by electron microscopy. The integrity of the leucine repeat appears to be essential for the formation and nuclear retention of these inclusions. Together, our results demonstrate the multifunctional nature of pIX and provide new insights into Ad biology.
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