Evidence map›Paper›PMID 31624094›Full record

ArticleScience (New York, N.Y.)2019

Architecture of African swine fever virus and implications for viral assembly.

Nan Wang, Dongming Zhao, Jialing Wang, Yangling Zhang, Ming Wang, Yan Gao, Fang Li, Jingfei Wang, Zhigao Bu, Zihe Rao and 1 more

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Science (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 284 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
284citing papers in PubMed, 1 pooled it
53.7field-weighted citation impact, top 1% 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

284 citing papers in PubMed, 1 synthesis or guideline pooled it, 460 citations in OpenAlex.

  1. Pooled it
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  10. Why did some viruses evolve to be giants while others did not?Proceedings of the National Academy of Sciences of the United States of America · 2026
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224 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Nan WangCAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.ORCID http://orcid.org/0000-0002-9936-9179
Dongming ZhaoState Key Laboratory of Veterinary Biotechnology and National High Containment Laboratory for Animal Diseases Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China.ORCID http://orcid.org/0000-0001-7161-6214
Jialing WangCAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.ORCID http://orcid.org/0000-0003-3552-881X
Yangling ZhangCAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.ORCID http://orcid.org/0000-0001-6933-0540
Ming WangState Key Laboratory of Veterinary Biotechnology and National High Containment Laboratory for Animal Diseases Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China.
Yan GaoShanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Fang LiState Key Laboratory of Veterinary Biotechnology and National High Containment Laboratory for Animal Diseases Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China.
Jingfei WangState Key Laboratory of Veterinary Biotechnology and National High Containment Laboratory for Animal Diseases Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China.ORCID http://orcid.org/0000-0003-1035-1069
Zhigao BuState Key Laboratory of Veterinary Biotechnology and National High Containment Laboratory for Animal Diseases Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China. xiangxi@ibp.ac.cn buzhigao@caas.cn raozh@tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-9242-4211
Zihe RaoCAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. xiangxi@ibp.ac.cn buzhigao@caas.cn raozh@tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-9866-2384
Xiangxi WangCAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. xiangxi@ibp.ac.cn buzhigao@caas.cn raozh@tsinghua.edu.cn.ORCID http://orcid.org/0000-0003-0635-278X
Chinese Academy of Sciences · CNHarbin Veterinary Research Institute · CNShanghaiTech University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

African swine fever virus (ASFV) is a giant and complex DNA virus that causes a highly contagious and often lethal swine disease for which no vaccine is available. Using an optimized image reconstruction strategy, we solved the ASFV capsid structure up to 4.1 angstroms, which is built from 17,280 proteins, including one major (p72) and four minor (M1249L, p17, p49, and H240R) capsid proteins organized into pentasymmetrons and trisymmetrons. The atomic structure of the p72 protein informs putative conformational epitopes, distinguishing ASFV from other nucleocytoplasmic large DNA viruses. The minor capsid proteins form a complicated network below the outer capsid shell, stabilizing the capsid by holding adjacent capsomers together. Acting as core organizers, 100-nanometer-long M1249L proteins run along each edge of the trisymmetrons that bridge two neighboring pentasymmetrons and form extensive intermolecular networks with other capsid proteins, driving the formation of the capsid framework. These structural details unveil the basis of capsid stability and assembly, opening up new avenues for African swine fever vaccine development.

Indexed as

Virus AssemblyAfrican Swine Fever VirusAnimalsCapsidCapsid ProteinsCells, CulturedCryoelectron MicroscopyEpitopesModels, MolecularProtein ConformationProtein DomainsProtein FoldingProtein Structure, SecondarySwineVirioncapsid protein p72, African swine fever virusCapsid ProteinsEpitopes

Identifiers

PMID31624094
OpenAlexW2981124349

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.