Evidence map›Paper›PMID 27581436›Full record

ArticleClinical and vaccine immunology : CVI2016

Synergistic Neutralization of Pertussis Toxin by a Bispecific Antibody In Vitro and In Vivo.

Ellen K Wagner, Xianzhe Wang, Andre Bui, Jennifer A Maynard

Open access · diamondAbstract read
In one paragraph

Article in Clinical and vaccine immunology : CVI, 2016. 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
1.8field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
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  4. Structural basis for neutralizing antibody binding to pertussis toxin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. Review
  7. Structural Basis for Antibody Neutralization of Pertussis Toxin.bioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
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  17. Article
  18. Engineering therapeutic antibodies to combat infectious diseases.Current opinion in chemical engineering · 2018
    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

4 authors at 1 institution in 1 country.

Ellen K WagnerMcKetta Department of Chemical Engineering, The University of Texas at Austin, Austin, Texas, USA.
Xianzhe WangDepartment of Biochemistry, Institute of Cellular and Molecular Biology, The University of Texas at Austin, Austin, Texas, USA.
Andre BuiProteomics Facility, The University of Texas at Austin, Austin, Texas, USA.
Jennifer A MaynardMcKetta Department of Chemical Engineering, The University of Texas at Austin, Austin, Texas, USA maynard@che.utexas.edu.ORCID http://orcid.org/0000-0002-0363-8486
The University of Texas at Austin · US

Funding

Systematic evaluation of B. pertussis ACT’s role as a protective antigenR01AI122753 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI MAYNARD, JENNIFER A · 2016 to 2020
$1.9M
NIAID NIH HHS R01 AI122753
6 · The paper itself

Abstract

Bispecific antibodies are a rapidly growing class of therapeutic molecules, originally developed for the treatment of cancer but recently explored for the treatment of autoimmune and infectious diseases. Bordetella pertussis is a reemerging pathogen, and several of the key symptoms of infection are caused by the pertussis toxin (PTx). Two humanized antibodies, hu1B7 and hu11E6, bind distinct epitopes on PTx and, when coadministered, mitigate disease severity in murine and baboon models of infection. Here we describe the generation of a bispecific human IgG1 molecule combining the hu1B7 and hu11E6 binding sites via a knobs-in-holes design. The bispecific antibody showed binding activity equivalent to that of the antibody mixture in a competition enzyme-linked immunosorbent assay (ELISA). A CHO cell neutralization assay provided preliminary evidence for synergy between the two antibodies, while a murine model of PTx-induced leukocytosis definitively showed synergistic neutralization. Notably, the bispecific antibody retained the synergy observed for the antibody mixture, supporting the conclusion that synergy is due to simultaneous blockade of both the catalytic and receptor binding activities of pertussis toxin. These data suggest that a hu1B7/hu11E6 bispecific antibody is a viable alternative to an antibody mixture for pertussis treatment.

Indexed as

AnimalsAntibodies, BispecificAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedBinding Sites, AntibodyBordetella pertussisCHO CellsCricetinaeCricetulusDrug SynergismEnzyme-Linked Immunosorbent AssayEpitopesHumansImmunoglobulin GMiceNeutralization TestsAntibodies, BispecificAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedEpitopesImmunoglobulin GPertussis Toxin

Identifiers

PMID27581436
PMCPMC5098018
OpenAlexW2508073957

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.