Evidence map›Paper›PMID 31552676›Full record

ArticleFEBS letters2020

Stabilization of soluble high-affinity T-cell receptor with de novo disulfide bonds.

Flávio Sádio, Gerhard Stadlmayr, Katharina Stadlbauer, Maximilian Gräf, Agnes Scharrer, Florian Rüker, Gordana Wozniak-Knopp

Open access · hybridAbstract read
In one paragraph

Article in FEBS letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 31% 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

8 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Adoptive T-cell Immunotherapy: Perfecting Self-Defenses.Experientia supplementum (2012) · 2022
    Article
  7. Review
  8. 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

7 authors at 1 institution in 1 country.

Flávio SádioChristian Doppler Laboratory for Innovative Immunotherapeutics, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.
Gerhard StadlmayrChristian Doppler Laboratory for Innovative Immunotherapeutics, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.
Katharina StadlbauerChristian Doppler Laboratory for Innovative Immunotherapeutics, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.
Maximilian GräfChristian Doppler Laboratory for Innovative Immunotherapeutics, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.
Agnes ScharrerChristian Doppler Laboratory for Innovative Immunotherapeutics, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.
Florian RükerChristian Doppler Laboratory for Innovative Immunotherapeutics, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.
Gordana Wozniak-KnoppChristian Doppler Laboratory for Innovative Immunotherapeutics, Department of Biotechnology, University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.ORCID 0000-0002-4069-070X
Christian Doppler Laboratory for Thermoelectricity · AT

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Soluble T-cell receptors (TCRs) have recently gained visibility as target-recognition units of anticancer immunotherapeutic agents. Here, we improved the thermal stability of the well-expressed high-affinity A6 TCR by introducing pairs of cysteines in the invariable parts of the α- and β-chain. A mutant with a novel intradomain disulfide bond in each chain also tested superior to the wild-type in the accelerated stability assay. Binding of the mutant to the soluble cognate peptide (cp)-MHC and to the peptide-loaded T2 cell line was equal to the wild-type A6 TCR. The same stabilization motif worked efficiently in TCRs with different specificities, such as DMF5 and 1G4. Altogether, the biophysical properties of the soluble TCR molecule could be improved, without affecting its expression level and antigen-binding specificity.

Indexed as

Amino Acid SubstitutionCell LineDisulfidesModels, MolecularProtein BindingProtein ConformationProtein StabilityReceptors, Antigen, T-CellSolubilityTransition TemperatureDisulfidesReceptors, Antigen, T-Cellnovel disulfide bondpMHC bindingsoluble TCRsstability engineering

Identifiers

PMID31552676
PMCPMC7027902
OpenAlexW2975889996

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.