Evidence map›Paper›PMID 24357008›Full record

ArticleAnalytical and bioanalytical chemistry2014

Sizing up large protein complexes by electrospray ionisation-based electrophoretic mobility and native mass spectrometry: morphology selective binding of Fabs to hepatitis B virus capsids.

Jessica Z Bereszczak, Marlene Havlik, Victor U Weiss, Martina Marchetti-Deschmann, Esther van Duijn, Norman R Watts, Paul T Wingfield, Guenter Allmaier, Alasdair C Steven, Albert J R Heck

Abstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. MASS SPECTROMETRY IN VIROLOGICAL SCIENCES.Mass spectrometry reviews · 2020
    Review
  9. Collision-Induced Unfolding Is Sensitive to the Polarity of Proteins and Protein Complexes.Journal of the American Society for Mass Spectrometry · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. 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

10 authors at 5 institutions in 3 countries.

Jessica Z BereszczakBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Marlene Havlik
Victor U Weiss
Martina Marchetti-Deschmann
Esther van Duijn
Norman R Watts
Paul T Wingfield
Guenter Allmaier
Alasdair C Steven
Albert J R Heck
TU Wien · ATUtrecht University · NLNational Institute of Arthritis and Musculoskeletal and Skin Diseases · USNational Institutes of Health · USProtein Express (United States) · US

Funding

Structural Biology Of Virus AssemblyZIAAR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2024
$19.2M
Structure And Assembly Of The Hepatitis B Nucleocapsid ProteinZIAAR041117 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2015
$5.0M
Intramural NIH HHS ZIA AR041117
6 · The paper itself

Abstract

The capsid of hepatitis B virus (HBV) is a major viral antigen and important diagnostic indicator. HBV capsids have prominent protrusions ('spikes') on their surface and are unique in having either T = 3 or T = 4 icosahedral symmetry. Mouse monoclonal and also human polyclonal antibodies bind either near the spike apices (historically the 'α-determinant') or in the 'floor' regions between them (the 'β-determinant'). Native mass spectrometry (MS) and gas-phase electrophoretic mobility molecular analysis (GEMMA) were used to monitor the titration of HBV capsids with the antigen-binding domain (Fab) of mAb 3120, which has long defined the β-determinant. Both methods readily distinguished Fab binding to the two capsid morphologies and could provide accurate masses and dimensions for these large immune complexes, which range up to ~8 MDa. As such, native MS and GEMMA provide valuable alternatives to a more time-consuming cryo-electron microscopy analysis for preliminary characterisation of virus-antibody complexes.

Indexed as

Antigen-Antibody ComplexAntigens, ViralBinding SitesCapsidHepatitis B virusHumansImmunoglobulin Fab FragmentsMass SpectrometryProtein BindingProtein Interaction Domains and MotifsSpectrometry, Mass, Electrospray IonizationAntigen-Antibody ComplexAntigens, ViralImmunoglobulin Fab Fragments

Identifiers

PMID24357008
PMCPMC4175414
OpenAlexW2142630383

What OpenQuestion holds

Textmetadata
LicenceTDM
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.