ArticleVirology2010
Virion incorporation of the herpes simplex virus type 1 tegument protein VP22 is facilitated by trans-Golgi network localization and is independent of interaction with glycoprotein E.
Article in Virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Review
- "Non-Essential" Proteins of HSV-1 with Essential Roles In Vivo: A Comprehensive Review.Viruses · 2020Review
- Alphaherpesvirus Major Tegument Protein VP22: Its Precise Function in the Viral Life Cycle.Frontiers in microbiology · 2020Review
- Article
- Article
- The C-Terminus of Epstein-Barr Virus BRRF2 Is Required for its Proper Localization and Efficient Virus Production.Frontiers in microbiology · 2017Article
- VP22 core domain from Herpes simplex virus 1 reveals a surprising structural conservation in both the Alpha- and Gammaherpesvirinae subfamilies.The Journal of general virology · 2015Article
- Deletion of the ORF9p acidic cluster impairs the nuclear egress of varicella-zoster virus capsids.Journal of virology · 2015Article
- Elucidation of the block to herpes simplex virus egress in the absence of tegument protein UL16 reveals a novel interaction with VP22.Journal of virology · 2014Article
- The Us2 gene product of herpes simplex virus 2 is a membrane-associated ubiquitin-interacting protein.Journal of virology · 2013Article
- Herpes simplex virus membrane proteins gE/gI and US9 act cooperatively to promote transport of capsids and glycoproteins from neuron cell bodies into initial axon segments.Journal of virology · 2013Article
- Interaction and interdependent packaging of tegument protein UL11 and glycoprotein e of herpes simplex virus.Journal of virology · 2011Article
- Herpes simplex virus glycoproteins gB and gD function in a redundant fashion to promote secondary envelopment.Journal of virology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
HSV-1 virions contain a proteinaceous layer termed the tegument that lies between the nucleocapsid and viral envelope. The molecular mechanisms that facilitate incorporation of tegument proteins are poorly characterized. The tegument protein VP22 interacts with VP16 and the cytoplasmic tail of glycoprotein E (gE). Virion incorporation of VP22 occurs independently of interaction with VP16; however, the contribution of gE binding remains undefined. Site-directed mutagenesis was used to identify VP22 mutants which abrogate interaction with gE but retain VP16 binding. Virion incorporation assays demonstrated that failure to bind gE did not abrogate VP22 packaging. A region of VP22 which binds to both VP16 and gE failed to be packaged efficiently, with wild-type levels of incorporation only attained when residues 43-86 of VP22 were present. Mutational analysis of an acidic cluster of amino acids within this region indicates that this motif facilitates trans-Golgi network (TGN) localization and optimal virion incorporation of VP22.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.