Evidence map›Paper›PMID 26151485›Full record

ArticleJournal of molecular biology2016

Charge Detection Mass Spectrometry Identifies Preferred Non-Icosahedral Polymorphs in the Self-Assembly of Woodchuck Hepatitis Virus Capsids.

Elizabeth E Pierson, David Z Keifer, Alexander A Kukreja, Joseph C-Y Wang, Adam Zlotnick, Martin F Jarrold

Abstract read
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Virus Assembly Pathways: Straying Away but Not Too Far.Small (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Hepatitis B Virus Capsid Completion Occurs through Error Correction.Journal of the American Chemical Society · 2017
    Article
  20. Mass and Charge Measurements on Heavy Ions.Mass spectrometry (Tokyo, Japan) · 2017
    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

6 authors at 1 institution in 1 country.

Elizabeth E PiersonDepartment of Chemistry and Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA.
David Z KeiferDepartment of Chemistry and Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA.
Alexander A KukrejaDepartment of Chemistry and Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA.
Joseph C-Y WangDepartment of Chemistry and Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA.
Adam ZlotnickDepartment of Chemistry and Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA. Electronic address: zlotnic@indiana.edu.
Martin F JarroldDepartment of Chemistry and Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, USA. Electronic address: mfj@indiana.edu.
Indiana University Bloomington · US

Funding

The Biophysics of Virus Capsid AssemblyR01AI077688 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI ZLOTNICK, ADAM · 2009 to 2013
$1.5M
The Biophysics of Virus Capsid AssemblyR56AI077688 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI ZLOTNICK, ADAM · 2014 to 2014
$347k
NIAID NIH HHS R01 AI077688NIAID NIH HHS R56 AI077688NIAID NIH HHS R56-AI077688
6 · The paper itself

Abstract

Woodchuck hepatitis virus (WHV) is prone to aberrant assembly in vitro and can form a broad distribution of oversized particles. Characterizing aberrant assembly products is challenging because they are both large and heterogeneous. In this work, charge detection mass spectrometry (CDMS) is used to measure the distribution of WHV assembly products. CDMS is a single-particle technique where the masses of individual ions are determined from simultaneous measurement of each ion's charge and m/z (mass-to-charge) ratio. Under relatively aggressive, assembly promoting conditions, roughly half of the WHV assembly products are T=4 capsids composed of exactly 120 dimers while the other half are a broad distribution of larger species that extends to beyond 210 dimers. There are prominent peaks at around 132 dimers and at 150 dimers. In part, the 150 dimer complex can be attributed to elongating a T=4 capsid along its 5-fold axis by adding a ring of hexamers. However, most of the other features cannot be explained by existing models for hexameric defects. Cryo-electron microscopy provides evidence of elongated capsids. However, image analysis reveals that many of them are not closed but have "spiral-like" morphologies. The CDMS data indicate that oversized capsids have a preference for growth by addition of 3 or 4 dimers, probably by completion of hexameric vertices.

Indexed as

Mass SpectrometryVirus AssemblyCapsidCryoelectron MicroscopyHepatitis B Virus, WoodchuckVirioncapsid assemblymass spectrometryself-assemblywoodchuck hepatitis virus

Identifiers

PMID26151485
PMCPMC5653371
OpenAlexW748729939

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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.