Evidence map›Paper›PMID 9114042›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Peptide-specific killing of antigen-presenting cells by a recombinant antibody-toxin fusion protein targeted to major histocompatibility complex/peptide class I complexes with T cell receptor-like specificity.

Y Reiter, A Di Carlo, L Fugger, J Engberg, I Pastan

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Targeting the MHC Ligandome by Use of TCR-Like Antibodies.Antibodies (Basel, Switzerland) · 2019
    Review
  3. Review
  4. Article
  5. Article
  6. Strategies to genetically engineer T cells for cancer immunotherapy.Cancer immunology, immunotherapy : CII · 2016
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

5 authors at 3 institutions in 1 country.

Y ReiterLaboratory of Molecular Biology, Division of Basic Sciences, National Cancer Institute, Building 37, Room 4E16, National Institutes of Health, Bethesda, MD 20892-4255, USA.
A Di Carlo
L Fugger
J Engberg
I Pastan
National Cancer Institute · USNational University · USNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specificity in the immune system is dictated and regulated by specific recognition of peptide/major histocompatibility complex (MHC) complexes by the T cell receptor. Such peptide/MHC complexes are a desirable target for novel approaches in immunotherapy because of their highly restricted fine specificity. Recently, phage display was used to isolate an antibody that has T cell receptor-like specificity. It recognizes mouse MHC class I H-2Kk molecules complexed with a H-2Kk-restricted influenza virus-derived hemagglutinin peptide (Ha255-262) but does not bind to class I H-2Kk alone, peptide alone, or H-2Kk complexed with other peptides. We have used this antibody to make a recombinant antibody-toxin fusion protein (immunotoxin) and show herein that it specifically kills antigen-presenting cells in a peptide-dependent manner and with T cell receptor-like specificity. We find a striking correlation between the fine specificity of binding of the antibody and the cytotoxic activity of the recombinant immunotoxin. We also show specific killing of influenza virus-infected target cells. The results suggest that it should be possible to develop novel immunotherapeutic strategies against human cancer by making recombinant antibodies that will recognize cancer-related peptides complexed with MHC class I molecules on the surface of cancer cells and using these to deliver toxins, radioisotopes, or cytotoxic drugs to the cancer cells.

Indexed as

ADP Ribose TransferasesHistocompatibility Antigens Class IVirulence FactorsAnimalsAntibodiesAntigen-Presenting CellsBacterial ToxinsCytotoxicity, ImmunologicExotoxinsH-2 AntigensHumansImmunotherapyImmunotoxinsInfluenza A virusMicePeptidesADP Ribose TransferasesAntibodiesBacterial ToxinsExotoxinsH-2 AntigensH-2K(K) antigenHistocompatibility Antigens Class IImmunotoxinsPeptidesPoly(ADP-ribose) PolymerasesPseudomonas aeruginosa Exotoxin AReceptors, Antigen, T-CellRecombinant Fusion ProteinsVirulence Factors

Identifiers

PMID9114042
PMCPMC20775
OpenAlexW2039312118

What OpenQuestion holds

Textmetadata
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.