ArticleVaccine2008
Domain specificity of the human antibody response to Bacillus anthracis protective antigen.
Article in Vaccine, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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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.
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
16 citing papers in PubMed, 29 citations in OpenAlex.
- Anthrax Vaccines in the 21st Century.Vaccines · 2024Review
- Constructing and transient expression of a gene cassette containing edible vaccine elements and shigellosis, anthrax and cholera recombinant antigens in tomato.Molecular biology reports · 2018Article
- Insights From Analysis of Human Antigen-Specific Memory B Cell Repertoires.Frontiers in immunology · 2018Review
- The promise and challenge of epitope-focused vaccines.Human vaccines & immunotherapeutics · 2016Article
- Epitope-focused peptide immunogens in human use adjuvants protect rabbits from experimental inhalation anthrax.Vaccine · 2015Article
- Identification and validation of a linear protective neutralizing epitope in the β-pore domain of alpha toxin.PloS one · 2015Article
- Identification of peptide sequences as a measure of Anthrax vaccine stability during storage.Human vaccines & immunotherapeutics · 2014Article
- Recombinant vaccine displaying the loop-neutralizing determinant from protective antigen completely protects rabbits from experimental inhalation anthrax.Clinical and vaccine immunology : CVI · 2013Article
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- Recombinant anthrax toxin receptor-Fc fusion proteins produced in plants protect rabbits against inhalational anthrax.Antimicrobial agents and chemotherapy · 2011Article
- Vaccination of rhesus macaques with the anthrax vaccine adsorbed vaccine produces a serum antibody response that effectively neutralizes receptor-bound protective antigen in vitro.Clinical and vaccine immunology : CVI · 2010Article
- An anthrax subunit vaccine candidate based on protective regions of Bacillus anthracis protective antigen and lethal factor.Vaccine · 2010Article
- Analysis of antibody responses to protective antigen-based anthrax vaccines through use of competitive assays.Clinical and vaccine immunology : CVI · 2010Article
- A heterologous helper T-cell epitope enhances the immunogenicity of a multiple-antigenic-peptide vaccine targeting the cryptic loop-neutralizing determinant of Bacillus anthracis protective antigen.Infection and immunity · 2009Article
- Frequency and domain specificity of toxin-neutralizing paratopes in the human antibody response to anthrax vaccine adsorbed.Infection and immunity · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Protective antigen (PA) is the cell surface recognition moiety of the Bacillus anthracis A-B toxin system, and the active immunogenic component in the currently licensed human anthrax vaccine (BioThrax, or AVA). The serum antibody response to the PA protein is polyclonal and complex both in terms of the antibody combining sites utilized to bind PA and the PA-associated epitopes recognized. We have cloned, sequenced, and expressed a large panel of PA-specific human monoclonal antibodies from seven AVA-immunized donors. Dot blots, Western blots, and radiolabeled antigen capture assays employing both proteolytic fragments of PA and engineered PA sub-domain fusion proteins were used to determine the region (domain) of the PA monomer to which each of the cloned human antibodies bound. The domain specificity of the isolated monoclonals was highly biased towards the amino-terminal 20kDa fragment of PA (PA(20)), with the majority (62%) of independently arising antibody clones reacting with determinants located on this PA fragment. A similar bias in domain specificity was also demonstrated in the serum response of AVA-vaccinated donors. Since PA(20) is cleaved from the remainder of the monomer rapidly following cell surface binding and has no known role in the intoxication process, the immunodominance of PA(20)-associated epitopes may directly affect the efficacy of PA-based anthrax vaccines.
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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.