Evidence map›Paper›PMID 21191022›Full record

ArticleJournal of virology2011

Rhesus rotavirus entry into a polarized epithelium is endocytosis dependent and involves sequential VP4 conformational changes.

Marie Wolf, Phuoc T Vo, Harry B Greenberg

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Drebrin restricts rotavirus entry by inhibiting dynamin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Review
  9. Article
  10. Carbohydrate recognition by rotaviruses.Journal of structural and functional genomics · 2014
    Review
  11. Article
  12. Article
  13. Genome-wide RNAi screen reveals a role for the ESCRT complex in rotavirus cell entry.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Marie WolfStanford University, VA-PAHCS, 3801 Miranda Avenue (154 C), Building 101, Room C4-181, Palo Alto, CA 94304, USA. mmwolf@stanford.edu
Phuoc T Vo
Harry B Greenberg
Stanford University · US

Funding

Proteomics/GenomicsP30DK056339 · NIDDK · STANFORD UNIVERSITY · PI GREENBERG, HARRY BERNARD · 2001 to 2010
$10.4M
VIRAL GASTROENTERITIS--BASIS OF PROTECTION AND VIRULENCER01AI021362 · NIAID · STANFORD UNIVERSITY · PI GREENBERG, HARRY BERNARD · 1989 to 2014
$5.4M
NIAID NIH HHS R01 AI-021362NIAID NIH HHS R01 AI021362NIDDK NIH HHS P30 DK056339NIDDK NIH HHS P30 DK56339-08
6 · The paper itself

Abstract

Rotavirus (RV) cell entry is an incompletely understood process, involving VP4 and VP7, the viral proteins composing the outermost layer of the nonenveloped RV triple-layered icosahedral particle (TLP), encasing VP6. VP4 can exist in three conformational states: soluble, cleaved spike, and folded back. In order to better understand the events leading to RV entry, we established a detection system to image input virus by monitoring the rhesus RV (RRV) antigens VP4, VP6, and VP7 at very early times postinfection. We provide evidence that decapsidation occurs directly after cell membrane penetration. We also demonstrate that several VP4 and VP7 conformational changes take place during entry. In particular, we detected, for the first time, the generation of folded-back VP5 in the context of the initiation of infection. Folded-back VP5 appears to be limited to the entry step. We furthermore demonstrate that RRV enters the cell cytoplasm through an endocytosis pathway. The endocytosis hypothesis is supported by the colocalization of RRV antigens with the early endosome markers Rab4 and Rab5. Finally, we provide evidence that the entry process is likely dependent on the endocytic Ca(2+) concentration, as bafilomycin A1 treatment as well as an augmentation of the extracellular calcium reservoir using CaEGTA, which both lead to an elevated intraendosomal calcium concentration, resulted in the accumulation of intact virions in the actin network. Together, these findings suggest that internalization, decapsidation, and cell membrane penetration involve endocytosis, calcium-dependent uncoating, and VP4 conformational changes, including a fold-back.

Indexed as

EndocytosisProtein FoldingVirus InternalizationAnimalsAntigens, ViralCalciumCapsid ProteinsCell LineEndothelial CellsMacaca mulattaProtein Conformationrab4 GTP-Binding Proteinsrab5 GTP-Binding ProteinsRotavirusAntigens, ViralCalciumCapsid Proteinsrab4 GTP-Binding Proteinsrab5 GTP-Binding ProteinsVP4 protein, RotavirusVP6 protein, RotavirusVP7 protein, Rotavirus

Identifiers

PMID21191022
PMCPMC3067957
OpenAlexW2103006232

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.