Evidence map›Paper›PMID 28795465›Full record

ArticleProtein science : a publication of the Protein Society2017

A molecular breadboard: Removal and replacement of subunits in a hepatitis B virus capsid.

Lye Siang Lee, Nicholas Brunk, Daniel G Haywood, David Keifer, Elizabeth Pierson, Panagiotis Kondylis, Joseph Che-Yen Wang, Stephen C Jacobson, Martin F Jarrold, Adam Zlotnick

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

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  12. Physical virology: From virus self-assembly to particle mechanics.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2020
    Review
  13. Article
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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

10 authors.

Lye Siang LeeMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, 47405.
Nicholas BrunkMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, 47405.
Daniel G HaywoodDepartment of Chemistry, Indiana University, Bloomington, Indiana, 47405.
David KeiferDepartment of Chemistry, Indiana University, Bloomington, Indiana, 47405.
Elizabeth PiersonDepartment of Chemistry, Indiana University, Bloomington, Indiana, 47405.
Panagiotis KondylisDepartment of Chemistry, Indiana University, Bloomington, Indiana, 47405.
Joseph Che-Yen WangMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, 47405.
Stephen C JacobsonDepartment of Chemistry, Indiana University, Bloomington, Indiana, 47405.
Martin F JarroldDepartment of Chemistry, Indiana University, Bloomington, Indiana, 47405.
Adam ZlotnickMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, 47405.ORCID http://orcid.org/0000-0001-9945-6267

Funding

Multimode Observation of Virus Capsid AssemblyR01AI118933 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI Adam Zlotnick · 2016 to 2026
$4.0M
NIAID NIH HHS R01 AI118933
6 · The paper itself

Abstract

Hepatitis B virus (HBV) core protein is a model system for studying assembly and disassembly of icosahedral structures. Controlling disassembly will allow re-engineering the 120 subunit HBV capsid, making it a molecular breadboard. We examined removal of subunits from partially crosslinked capsids to form stable incomplete particles. To characterize incomplete capsids, we used two single molecule techniques, resistive-pulse sensing and charge detection mass spectrometry. We expected to find a binomial distribution of capsid fragments. Instead, we found a preponderance of 3 MDa complexes (90 subunits) and no fragments smaller than 3 MDa. We also found 90-mers in the disassembly of uncrosslinked HBV capsids. 90-mers seem to be a common pause point in disassembly reactions. Partly explaining this result, graph theory simulations have showed a threshold for capsid stability between 80 and 90 subunits. To test a molecular breadboard concept, we showed that missing subunits could be refilled resulting in chimeric, 120 subunit particles. This result may be a means of assembling unique capsids with functional decorations.

Indexed as

Boron CompoundsCapsidComputer SimulationEthylmaleimideFluorescent DyesHepatitis B virusMass SpectrometryMolecular WeightMonte Carlo MethodProtein MultimerizationProtein SubunitsSodium ChlorideStatic ElectricityUreaViral Core Proteins4,4-difluoro-4-bora-3a,4a-diaza-s-indaceneBoron CompoundsEthylmaleimideFluorescent DyesProtein SubunitsSodium ChlorideUreaViral Core Proteinscharge detection mass spectrometrydisassemblynanofluidicsresistive pulse sensingself-assembly

Identifiers

PMID28795465
PMCPMC5654856

What OpenQuestion 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 OpenQuestion graph.