Evidence map›Paper›PMID 19622744›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding.

Tom S Y Guu, Zheng Liu, Qiaozhen Ye, Douglas A Mata, Kunpeng Li, Changcheng Yin, Jingqiang Zhang, Yizhi Jane Tao

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

130 citing papers in PubMed, 249 citations in OpenAlex.

  1. Review
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  9. Article
  10. Single-Particle Cryo-EM to Investigate Nonenveloped Virus-Like Particles.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  11. Cryo-Electron Microscopy in the Study of Antiviral Innate Immunity.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  12. EngineeringVaccines · 2024
    Review
  13. Cell binding tropism of rat hepatitis E virus is a pivotal determinant of its zoonotic transmission to humans.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Hepatitis E virus: from innate sensing to adaptive immune responses.Nature reviews. Gastroenterology & hepatology · 2024
    Review
  15. Review
  16. Article
  17. Review
  18. Hepatitis E Virus: What More Do We Need to Know?Medicina (Kaunas, Lithuania) · 2024
    Review
  19. Review
  20. Review

70 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 2 countries.

Tom S Y GuuDepartment of Biochemistry and Cell Biology, Rice University, Houston, TX 77005, USA.
Zheng Liu
Qiaozhen Ye
Douglas A Mata
Kunpeng Li
Changcheng Yin
Jingqiang Zhang
Yizhi Jane Tao
Rice University · USPeking University · CNSun Yat-sen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hepatitis E virus (HEV), a small, non-enveloped RNA virus in the family Hepeviridae, is associated with endemic and epidemic acute viral hepatitis in developing countries. Our 3.5-A structure of a HEV-like particle (VLP) shows that each capsid protein contains 3 linear domains that form distinct structural elements: S, the continuous capsid; P1, 3-fold protrusions; and P2, 2-fold spikes. The S domain adopts a jelly-roll fold commonly observed in small RNA viruses. The P1 and P2 domains both adopt beta-barrel folds. Each domain possesses a potential polysaccharide-binding site that may function in cell-receptor binding. Sugar binding to P1 at the capsid protein interface may lead to capsid disassembly and cell entry. Structural modeling indicates that native T = 3 capsid contains flat dimers, with less curvature than those of T = 1 VLP. Our findings significantly advance the understanding of HEV molecular biology and have application to the development of vaccines and antiviral medications.

Indexed as

Virus AssemblyAmino Acid SequenceBinding SitesCapsid ProteinsDimerizationHepatitis E virusModels, MolecularMolecular Sequence DataPolysaccharidesProtein Structure, SecondaryProtein Structure, TertiaryReceptors, VirusVirionCapsid ProteinsPolysaccharidesReceptors, Virus

Identifiers

PMID19622744
PMCPMC2722310
OpenAlexW2106555961

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.