Evidence map›Paper›PMID 33500404›Full record

ArticleNature communications2021

Asymmetrizing an icosahedral virus capsid by hierarchical assembly of subunits with designed asymmetry.

Zhongchao Zhao, Joseph Che-Yen Wang, Mi Zhang, Nicholas A Lyktey, Martin F Jarrold, Stephen C Jacobson, Adam Zlotnick

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
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  7. Review
  8. Review
  9. Encoding hierarchical assembly pathways of proteins with DNA.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

7 authors.

Zhongchao ZhaoMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, IN, 47405, USA.ORCID 0000-0002-3736-6677
Joseph Che-Yen WangMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, IN, 47405, USA.
Mi ZhangDepartment of Chemistry, Indiana University, Bloomington, IN, 47405, USA.
Nicholas A LykteyDepartment of Chemistry, Indiana University, Bloomington, IN, 47405, USA.
Martin F JarroldDepartment of Chemistry, Indiana University, Bloomington, IN, 47405, USA.
Stephen C JacobsonDepartment of Chemistry, Indiana University, Bloomington, IN, 47405, USA.ORCID 0000-0003-2415-041X
Adam ZlotnickMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, IN, 47405, USA. azlotnic@indiana.edu.ORCID 0000-0001-9945-6267

Funding

Multimode Observation of Virus Capsid AssemblyR01AI118933 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI Adam Zlotnick · 2016 to 2026
$4.0M
The Structural Biology of HBVR01AI144022 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI ZLOTNICK, ADAM · 2019 to 2022
$1.5M
Single-Particle Analysis of Virus Capsid Assembly and Disassembly by Resistive-Pulse SensingR01GM129354 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI JACOBSON, STEPHEN C · 2018 to 2020
$925k
NIAID NIH HHS R01 AI118933NIAID NIH HHS R01 AI144022NIGMS NIH HHS R01 GM129354
6 · The paper itself

Abstract

Symmetrical protein complexes are ubiquitous in biology. Many have been re-engineered for chemical and medical applications. Viral capsids and their assembly are frequent platforms for these investigations. A means to create asymmetric capsids may expand applications. Here, starting with homodimeric Hepatitis B Virus capsid protein, we develop a heterodimer, design a hierarchical assembly pathway, and produce asymmetric capsids. In the heterodimer, the two halves have different growth potentials and assemble into hexamers. These preformed hexamers can nucleate co-assembly with other dimers, leading to Janus-like capsids with a small discrete hexamer patch. We can remove the patch specifically and observe asymmetric holey capsids by cryo-EM reconstruction. The resulting hole in the surface can be refilled with fluorescently labeled dimers to regenerate an intact capsid. In this study, we show how an asymmetric subunit can be used to generate an asymmetric particle, creating the potential for a capsid with different surface chemistries.

Indexed as

Models, MolecularVirus AssemblyCapsidCapsid ProteinsCryoelectron MicroscopyHepatitis B virusProtein MultimerizationRecombinant ProteinsCapsid ProteinsRecombinant Proteins

Identifiers

PMID33500404
PMCPMC7838286

What Socratic holds

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Registered trials

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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 Socratic graph.