ArticleInfection and immunity2000
Use of pertussis toxin encoded by ptx genes from Bordetella bronchiseptica to model the effects of antigenic drift of pertussis toxin on antibody neutralization.
Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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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.
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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.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Pangenomics-Driven Reverse Vaccinology for the Discovery of New Vaccine Candidates AgainstBioinformatics and biology insights · 2026Article
- Four single-basepair mutations in the ptx promoter of Bordetella bronchiseptica are sufficient to activate the expression of pertussis toxin.Scientific reports · 2021Article
- Conservation of Ancient Genetic Pathways for Intracellular Persistence Among Animal Pathogenic Bordetellae.Frontiers in microbiology · 2019Article
- Bordetella bronchiseptica in the immunosuppressed population - a case series and review.Mediterranean journal of hematology and infectious diseases · 2014Article
- Population diversity among Bordetella pertussis isolates, United States, 1935-2009.Emerging infectious diseases · 2012Article
- Interleukin-1 receptor signaling is required to overcome the effects of pertussis toxin and for efficient infection- or vaccination-induced immunity against Bordetella pertussis.Infection and immunity · 2011Article
- Characterization of a key neutralizing epitope on pertussis toxin recognized by monoclonal antibody 1B7.Biochemistry · 2009Article
- Pathogen proteins eliciting antibodies do not share epitopes with host proteins: a bioinformatics approach.PloS one · 2007Article
- Pertussis toxin inhibits neutrophil recruitment to delay antibody-mediated clearance of Bordetella pertussis.The Journal of clinical investigation · 2005Article
- Bordetella pertussis: the intersection of genomics and pathobiology.CMAJ : Canadian Medical Association journal = journal de l'Association medicale canadienne · 2005Review
- Antigenic divergence suggested by correlation between antigenic variation and pulsed-field gel electrophoresis profiles of Bordetella pertussis isolates in Japan.Journal of clinical microbiology · 2004Article
- Polymorphisms of the fimbria fim3 gene of Bordetella pertussis strains isolated in Canada.Journal of clinical microbiology · 2004Article
- Polymorphism of Bordetella pertussis isolates circulating for the last 10 years in France, where a single effective whole-cell vaccine has been used for more than 30 years.Journal of clinical microbiology · 2001Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently, concern has been voiced about the potential effect that antigenic divergence of circulating strains of Bordetella pertussis might have on the efficacy of pertussis vaccines. In order to model antigenic drift of pertussis toxin, a critical component of many pertussis vaccines, and to examine the effects of such drift on antibody neutralization, we engineered a strain of B. pertussis to produce a variant pertussis toxin molecule that contains many of the amino acid changes found in the toxin encoded by Bordetella bronchiseptica ptx genes. This altered form of the toxin, which is efficiently secreted by B. pertussis and which displays significant biological activity, was found to be neutralized by antibodies induced by vaccination as readily as toxin produced by wild-type B. pertussis. These findings suggest that significant amino acid changes in the pertussis toxin sequence can occur without drastically altering the ability of antibodies to recognize and neutralize the toxin molecule.
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