Evidence map›Paper›PMID 28074040›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Potent neutralization of hepatitis A virus reveals a receptor mimic mechanism and the receptor recognition site.

Xiangxi Wang, Ling Zhu, Minghao Dang, Zhongyu Hu, Qiang Gao, Shuai Yuan, Yao Sun, Bo Zhang, Jingshan Ren, Abhay Kotecha and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Hepatitis A virus infection.Nature reviews. Disease primers · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

15 authors at 6 institutions in 2 countries.

Xiangxi WangNational Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China; xiangxi@ibp.ac.cn liz@strubi.ox.ac.uk dave@strubi.ox.ac.uk raozh@xtal.tsinghua.edu.cn.
Ling ZhuDivision of Structural Biology, University of Oxford, Oxford OX3 7BN, United Kingdom.
Minghao DangNational Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China.
Zhongyu HuNational Institutes for Food and Drug Control, Beijing 100050, China.
Qiang GaoNational Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China.
Shuai YuanNational Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China.
Yao SunNational Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China.
Bo ZhangSinovac Biotech Co., Ltd., Beijing 100085, China.
Jingshan RenDivision of Structural Biology, University of Oxford, Oxford OX3 7BN, United Kingdom.
Abhay KotechaDivision of Structural Biology, University of Oxford, Oxford OX3 7BN, United Kingdom.
Thomas S WalterDivision of Structural Biology, University of Oxford, Oxford OX3 7BN, United Kingdom.
Junzhi WangNational Institutes for Food and Drug Control, Beijing 100050, China.
Elizabeth E FryDivision of Structural Biology, University of Oxford, Oxford OX3 7BN, United Kingdom; xiangxi@ibp.ac.cn liz@strubi.ox.ac.uk dave@strubi.ox.ac.uk raozh@xtal.tsinghua.edu.cn.
David I StuartDivision of Structural Biology, University of Oxford, Oxford OX3 7BN, United Kingdom; xiangxi@ibp.ac.cn liz@strubi.ox.ac.uk dave@strubi.ox.ac.uk raozh@xtal.tsinghua.edu.cn.
Zihe RaoNational Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China; xiangxi@ibp.ac.cn liz@strubi.ox.ac.uk dave@strubi.ox.ac.uk raozh@xtal.tsinghua.edu.cn.
Institute of Biophysics · CNUniversity of Oxford · GBNational Institutes for Food and Drug Control · CNDiamond Light Source · GBSinovac Biotech · CNTsinghua University · CN

Funding

Medical Research Council G1100525Medical Research Council MR/N00065X/1Wellcome TrustWellcome Trust 060208/Z/00/ZWellcome Trust 090532/Z/07/ZWellcome Trust 093305/Z/10/Z
6 · The paper itself

Abstract

Hepatitis A virus (HAV) infects ∼1.4 million people annually and, although there is a vaccine, there are no licensed therapeutic drugs. HAV is unusually stable (making disinfection problematic) and little is known of how it enters cells and releases its RNA. Here we report a potent HAV-specific monoclonal antibody, R10, which neutralizes HAV infection by blocking attachment to the host cell. High-resolution cryo-EM structures of HAV full and empty particles and of the complex of HAV with R10 Fab reveal the atomic details of antibody binding and point to a receptor recognition site at the pentamer interface. These results, together with our observation that the R10 Fab destabilizes the capsid, suggest the use of a receptor mimic mechanism to neutralize virus infection, providing new opportunities for therapeutic intervention.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, NeutralizingBinding SitesCapsidCapsid ProteinsFemaleHepatitis A virusHumansImmunoglobulin Fab FragmentsMiceMice, Inbred BALB CAntibodies, MonoclonalAntibodies, NeutralizingCapsid ProteinsImmunoglobulin Fab Fragmentsentryneutralizing mechanismpicornavirusreceptor recognitionuncoating

Identifiers

PMID28074040
PMCPMC5278457
OpenAlexW2569156111

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.