Evidence map›Paper›PMID 34465620›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Molecular mechanism of capsid disassembly in hepatitis B virus.

Zhaleh Ghaemi, Martin Gruebele, Emad Tajkhorshid

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
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  3. Article
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  11. Understanding Virus Structure and Dynamics through Molecular Simulations.Journal of chemical theory and computation · 2023
    Review
  12. Article
  13. Article
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  15. Review
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.

Zhaleh GhaemiDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801.ORCID 0000-0002-3690-7005
Martin GruebeleDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801; emad@illinois.edu mgruebel@illinois.edu.ORCID 0000-0001-9291-8123
Emad TajkhorshidDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801; emad@illinois.edu mgruebel@illinois.edu.ORCID 0000-0001-8434-1010
University of Illinois Urbana-Champaign · US

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
Protein refolding and transient aggregate formation studied by very fast pressureR01GM093318 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GRUEBELE, MARTIN · 2010 to 2020
$3.1M
NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM093318
6 · The paper itself

Abstract

The disassembly of a viral capsid leading to the release of its genetic material into the host cell is a fundamental step in viral infection. In hepatitis B virus (HBV), the capsid consists of identical protein monomers that dimerize and then arrange themselves into pentamers or hexamers on the capsid surface. By applying atomistic molecular dynamics simulation to an entire solvated HBV capsid subjected to a uniform mechanical stress protocol, we monitor the capsid-disassembly process and analyze the process down to the level of individual amino acids in 20 independent simulation replicas. The strain of an isotropic external force, combined with structural fluctuations, causes structurally heterogeneous cracks to appear in the HBV capsid. Analysis of the monomer-monomer interfaces reveals that, in contrast to the expectation from purely mechanical considerations, the cracks mainly occur within hexameric sites, whereas pentameric sites remain largely intact. Only a small subset of the capsid protein monomers, different in each simulation, are engaged in each instance of disassembly. We identify specific residues whose interactions are most readily lost during disassembly; R127, I139, Y132, N136, A137, and V149 are among the hot spots at the interfaces between dimers that lie within hexamers, leading to disassembly. The majority of these hot-spot residues are conserved by evolution, hinting to their importance for disassembly by avoiding overstabilization of capsids.

Indexed as

Virus AssemblyBiopolymersCapsidGenes, ViralHepatitis B virusMolecular Dynamics SimulationMolecular StructureBiopolymersatomistic molecular dynamics simulationscapsid disassemblyhepatitis B virus

Identifiers

PMID34465620
PMCPMC8433540
OpenAlexW3198893438

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.