Evidence map›Paper›PMID 34305906›Full record

ArticleFrontiers in immunology2021

Molecular Insights of Nickel Binding to Therapeutic Antibodies as a Possible New Antibody Superantigen.

Chinh Tran-To Su, Wai-Heng Lua, Jun-Jie Poh, Wei-Li Ling, Joshua Yi Yeo, Samuel Ken-En Gan

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. 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

6 authors at 4 institutions in 1 country.

Chinh Tran-To SuAntibody & Product Development Lab, Experimental Drug Development Centre, Bioinformatics Institute, Agency for Science, Technology, and Research (ASTAR), Singapore, Singapore.
Wai-Heng LuaAntibody & Product Development Lab, Experimental Drug Development Centre, Bioinformatics Institute, Agency for Science, Technology, and Research (ASTAR), Singapore, Singapore.
Jun-Jie PohAntibody & Product Development Lab, Experimental Drug Development Centre, Bioinformatics Institute, Agency for Science, Technology, and Research (ASTAR), Singapore, Singapore.
Wei-Li LingAntibody & Product Development Lab, Experimental Drug Development Centre, Bioinformatics Institute, Agency for Science, Technology, and Research (ASTAR), Singapore, Singapore.
Joshua Yi YeoAntibody & Product Development Lab, Experimental Drug Development Centre, Bioinformatics Institute, Agency for Science, Technology, and Research (ASTAR), Singapore, Singapore.
Samuel Ken-En GanAntibody & Product Development Lab, Experimental Drug Development Centre, Bioinformatics Institute, Agency for Science, Technology, and Research (ASTAR), Singapore, Singapore.
Bioinformatics Institute · SGExperimental Drug Development Centre · SGAgency for Science, Technology and Research · SGJames Cook University Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The binding of nickel by immune proteins can manifest as Type IV contact dermatitis (Ni-specific T cells mediated) and less frequently as Type I hypersensitivity with both mechanisms remaining unknown to date. Since there are reports of patients co-manifesting the two hypersensitivities, a common mechanism may underlie both the TCR and IgE nickel binding. Focusing on Trastuzumab and Pertuzumab IgE variants as serendipitous investigation models, we found Ni-NTA interactions independent of Her2 binding to be due to glutamine stretches. These stretches are both Ni-inducible and in fixed pockets at the antibody complementarity-determining regions (CDRs) and framework regions (FWRs) of both the antibody heavy and light chains with influence from the heavy chain constant region. Comparisons with TCRs structures revealed similar interactions, demonstrating the possible underlying mechanism in selecting for Ni-binding IgEs and TCRs respectively. With the elucidation of the interaction, future therapeutic antibodies could also be sagaciously engineered to utilize such nickel binding for biotechnological purposes.

Indexed as

Antibodies, Monoclonal, HumanizedComplementarity Determining RegionsHEK293 CellsHumansHypersensitivityImmunoglobulin EImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionNickelReceptors, Antigen, T-CellSuperantigensTrastuzumabAntibodies, Monoclonal, HumanizedComplementarity Determining RegionsImmunoglobulin EImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionNickelpertuzumabReceptors, Antigen, T-CellSuperantigensTrastuzumaballergyantibodyglutamineIgEIgG1nickel (II)type I hypersensitivity

Identifiers

PMID34305906
PMCPMC8296638
OpenAlexW3182048773

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.