Evidence map›Paper›PMID 23940209›Full record

ArticleInfection and immunity2013

Identification of a human monoclonal antibody to replace equine diphtheria antitoxin for treatment of diphtheria intoxication.

Leila M Sevigny, Brian J Booth, Kirk J Rowley, Brett A Leav, Peter S Cheslock, Kerry A Garrity, Susan E Sloan, William Thomas, Gregory J Babcock, Yang Wang

Abstract read
In one paragraph

Article in Infection and immunity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Diphtheria antitoxin treatment: from pioneer to neglected.Memorias do Instituto Oswaldo Cruz · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Diphtheria Antitoxin Administration, Outcomes, and Safety: Response to a Diphtheria Outbreak in Cox's Bazar, Bangladesh.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2021
    Article
  10. Article
  11. Article
  12. Review
  13. Monoclonal antibodies as anti-infective products: a promising future?Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases · 2019
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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.

Leila M SevignyMassBiologics of the University of Massachusetts Medical School, Boston, Massachusetts, USA.
Brian J Booth
Kirk J Rowley
Brett A Leav
Peter S Cheslock
Kerry A Garrity
Susan E Sloan
William Thomas
Gregory J Babcock
Yang Wang

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diphtheria antitoxin (DAT) has been the cornerstone of the treatment of Corynebacterium diphtheriae infection for more than 100 years. Although the global incidence of diphtheria has declined steadily over the last quarter of the 20th century, the disease remains endemic in many parts of the world, and significant outbreaks still occur. DAT is an equine polyclonal antibody that is not commercially available in the United States and is in short supply globally. A safer, more readily available alternative to DAT would be desirable. In the current study, we obtained human monoclonal antibodies (hMAbs) directly from antibody-secreting cells in the circulation of immunized human volunteers. We isolated a panel of diverse hMAbs that recognized diphtheria toxoid, as well as a variety of recombinant protein fragments of diphtheria toxin. Forty-five unique hMAbs were tested for neutralization of diphtheria toxin in in vitro cytotoxicity assays with a 50% effective concentration of 0.65 ng/ml for the lead candidate hMAb, 315C4. In addition, 25 μg of 315C4 completely protected guinea pigs from intoxication in an in vivo lethality model, yielding an estimated relative potency of 64 IU/mg. In comparison, 1.6 IU of DAT was necessary for full protection from morbidity and mortality in this model. We further established that our lead candidate hMAb binds to the receptor-binding domain of diphtheria toxin and physically blocks the toxin from binding to the putative receptor, heparin-binding epidermal growth factor-like growth factor. The discovery of a specific and potent human neutralizing antibody against diphtheria toxin holds promise as a potential therapeutic.

Indexed as

AnimalsAntibodies, MonoclonalCell LineCorynebacterium diphtheriaeDiphtheriaDiphtheria AntitoxinDiphtheria ToxinDisease Models, AnimalEpitope MappingGuinea PigsHealthy VolunteersHumansImmunotherapyNeutralization TestsProtein BindingSurvival AnalysisAntibodies, MonoclonalDiphtheria AntitoxinDiphtheria Toxin

Identifiers

PMID23940209
PMCPMC3811848

What OpenQuestion holds

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Registered trials

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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.