ArticleBiochemistry2009
Characterization of a key neutralizing epitope on pertussis toxin recognized by monoclonal antibody 1B7.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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.
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.
Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- The Immunogenicity of Glutaraldehyde Inactivated PTx Is Determined by the Quantity of Neutralizing Epitopes.Vaccines · 2025Article
- Structural basis for neutralizing antibody binding to pertussis toxin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Development and Implementation of a Single Radial Diffusion Technique for Quality Control of Acellular Pertussis Vaccines.Vaccines · 2025Article
- Epitope Mapping Using Yeast Display and Next Generation Sequencing.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structural Basis for Antibody Neutralization of Pertussis Toxin.bioRxiv : the preprint server for biology · 2024Article
- Novel Strategies to Inhibit Pertussis Toxin.Toxins · 2022Review
- Review
- Humanised monoclonal antibodies neutralise pertussis toxin by receptor blockade and reduced retrograde trafficking.Cellular microbiology · 2018Article
- Characterization of Individual Human Antibodies That Bind Pertussis Toxin Stimulated by Acellular Immunization.Infection and immunity · 2018Article
- Synergistic Neutralization of Pertussis Toxin by a Bispecific Antibody In Vitro and In Vivo.Clinical and vaccine immunology : CVI · 2016Article
- Article
- A cocktail of humanized anti-pertussis toxin antibodies limits disease in murine and baboon models of whooping cough.Science translational medicine · 2015Article
- Rapid fine conformational epitope mapping using comprehensive mutagenesis and deep sequencing.The Journal of biological chemistry · 2015Article
- Increased Fab thermoresistance via VH-targeted directed evolution.Protein engineering, design & selection : PEDS · 2015Article
- Review
- Back to the future: recombinant polyclonal antibody therapeutics.Current opinion in chemical engineering · 2013Article
- Antibody nanoparticle dispersions formed with mixtures of crowding molecules retain activity and in vivo bioavailability.Journal of pharmaceutical sciences · 2012Article
- Restriction enzyme-free construction of random gene mutagenesis libraries in Escherichia coli.Analytical biochemistry · 2012Article
- Antibodies recognizing protective pertussis toxin epitopes are preferentially elicited by natural infection versus acellular immunization.Clinical and vaccine immunology : CVI · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Despite more than five decades of research and vaccination, infection by Bordetella pertussis remains a serious disease with no specific treatments or validated correlates of protective immunity. Of the numerous monoclonal antibodies binding pertussis toxin (PTx) that have been produced and characterized, murine IgG2a monoclonal antibody 1B7 is uniquely neutralizing in all in vitro assays and in vivo murine models of infection. 1B7 binds an epitope on the enzymatically active S1 subunit of PTx (PTx-S1) with some linear elements, but previous work with S1 scanning peptides, phage-displayed peptide libraries, and S1 truncation/deletion variants was unable to more precisely define the epitope. Using computational docking algorithms, alanine scanning mutagenesis, and surface plasmon resonance, we characterize the epitope bound by 1B7 on PTx-S1 in molecular detail and define energetically important interactions between residues at the interface. Six residues on PTx-S1 and six residues on 1B7 were identified that, when altered to alanine, resulted in variants with significantly reduced affinity for the native partner. Using this information, a model of the 1B7-S1 interaction was developed, indicating a predominantly conformational epitope located on the base of S1 near S4. The location of this epitope is consistent with previous data and is shown to be conserved across several naturally occurring strain variants, including PTx-S1A, -B (Tohama-I), -D, and -E (18-323) in addition to the catalytically inactive 9K/129G variant. This highly neutralizing but poorly immunogenic epitope may represent an important target for next-generation vaccine development, identification of immune correlates, and passive immunization strategies for pertussis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.