Evidence map›Paper›PMID 29757629›Full record

ArticleAnalytical chemistry2018

Signature of Antibody Domain Exchange by Native Mass Spectrometry and Collision-Induced Unfolding.

Yasunori Watanabe, Snezana Vasiljevic, Joel D Allen, Gemma E Seabright, Helen M E Duyvesteyn, Katie J Doores, Max Crispin, Weston B Struwe

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2018. 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
4.3field-weighted citation impact, top 5% 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, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. AgAnalytical chemistry · 2020
    Article
  9. Review
  10. Exploitation of glycosylation in enveloped virus pathobiology.Biochimica et biophysica acta. General subjects · 2019
    Review
  11. Quantitative collision-induced unfolding differentiates model antibody-drug conjugates.Protein science : a publication of the Protein Society · 2019
    Article
  12. Review
  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

8 authors at 4 institutions in 1 country.

Yasunori WatanabeBiological Sciences & The Institute for Life Sciences , University of Southampton , Southampton SO17 1BJ , United Kingdom.
Snezana Vasiljevic
Joel D AllenBiological Sciences & The Institute for Life Sciences , University of Southampton , Southampton SO17 1BJ , United Kingdom.
Gemma E SeabrightBiological Sciences & The Institute for Life Sciences , University of Southampton , Southampton SO17 1BJ , United Kingdom.
Helen M E DuyvesteynDivision of Structural Biology , Wellcome Centre for Human Genetics, University of Oxford , Roosevelt Drive , Oxford OX3 7BN , United Kingdom.
Katie J DooresDepartment of Infectious Diseases , King's College London , London SE1 9RT , United Kingdom.
Max CrispinBiological Sciences & The Institute for Life Sciences , University of Southampton , Southampton SO17 1BJ , United Kingdom.ORCID 0000-0002-1072-2694
University of Oxford · GBCentre for Human Genetics · GBUniversity of Southampton · GBKing's College London · GB

Funding

Support Component D/Vaccine Discovery, Concept to ClinicUM1AI100663 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BAROUCH, DAN H. · 2012 to 2018
$131.5M
NIAID NIH HHS UM1 AI100663
6 · The paper itself

Abstract

The development of domain-exchanged antibodies offers a route to high-affinity targeting to clustered multivalent epitopes, such as those associated with viral infections and many cancers. One strategy to generate these antibodies is to introduce mutations into target antibodies to drive domain exchange using the only known naturally occurring domain-exchanged anti-HIV (anti-human immunodeficiency virus) IgG1 antibody, 2G12 , as a template. Here, we show that domain exchange can be sensitively monitored by ion-mobility mass spectrometry and gas-phase collision-induced unfolding. Using native 2G12 and a mutated form that disrupts domain exchange such that it has a canonical IgG1 architecture ( 2G12 I19R ), we show that the two forms can be readily distinguished by their unfolding profiles. Importantly, the same signature of domain exchange is observed for both intact antibody and isolated Fab fragments. The development of a mass spectrometric method to detect antibody domain exchange will enable rapid screening and selection of candidate antibodies engineered to exhibit this and other unusual quaternary antibody architectures.

Indexed as

Antibodies, MonoclonalAntibodies, NeutralizingBroadly Neutralizing AntibodiesHIV AntibodiesHumansImmunoglobulin Fab FragmentsImmunoglobulin GMass SpectrometryMutant ProteinsProtein EngineeringProtein Structure, QuaternaryProtein Unfolding2G12 monoclonal antibodyAntibodies, MonoclonalAntibodies, NeutralizingBroadly Neutralizing AntibodiesHIV AntibodiesImmunoglobulin Fab FragmentsImmunoglobulin GMutant Proteins

Identifiers

PMID29757629
PMCPMC6008249
OpenAlexW2801861212

What OpenQuestion holds

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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.