Evidence map›Paper›PMID 19223482›Full record

ArticleInfection and immunity2009

Frequency and domain specificity of toxin-neutralizing paratopes in the human antibody response to anthrax vaccine adsorbed.

Donald Reason, Justine Liberato, Jinying Sun, Wendy Keitel, Jianhui Zhou

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

25 citing papers in PubMed, 34 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. The promise and challenge of epitope-focused vaccines.Human vaccines & immunotherapeutics · 2016
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Donald ReasonChildren's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609, USA. dreason@chori.org
Justine Liberato
Jinying Sun
Wendy Keitel
Jianhui Zhou
Baylor College of Medicine · US

Funding

CONSTRUCTION OF THE VACCINE CENTERC06RR016226 · NCRR · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI LUCAS, ALEXANDER H. · 2002 to 2002
$2.0M
Structural determinants of human immunity to anthraxR01AI057932 · NIAID · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI REASON, DONALD C · 2004 to 2008
$2.0M
Human monoclonal panel mimicking anthrax immune globulinR01AI066508 · NIAID · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI REASON, DONALD C · 2005 to 2005
$722k
NCRR NIH HHS C06 RR016226NCRR NIH HHS C06 RR-16226NIAID NIH HHS AI066508NIAID NIH HHS AI57932NIAID NIH HHS R01 AI057932NIAID NIH HHS R01 AI066508
6 · The paper itself

Abstract

Protective antigen (PA) is the cell surface recognition unit of the binary anthrax toxin system and the primary immunogenic component in both the current and proposed "next-generation" anthrax vaccines. Several studies utilizing animal models have indicated that PA-specific antibodies, acquired by either active or passive immunization, are sufficient to protect against infection with Bacillus anthracis. To investigate the human antibody response to anthrax immunization, we have established a large panel of human PA-specific monoclonal antibodies derived from multiple individuals vaccinated with the currently approved anthrax vaccine BioThrax. We have determined that although these antibodies bind PA in standard binding assays such as enzyme-linked immunosorbent assay, Western blotting, capture assays, and dot blots, less than 25% are capable of neutralizing lethal toxin (LT) in vitro. Nonneutralizing antibodies also fail to neutralize toxin when present in combination with other nonneutralizing paratopes. Although neutralizing antibodies recognize determinants throughout the PA monomer, they are significantly less common among those paratopes that bind to the immunodominant amino-terminal portion of the molecule. These findings demonstrate that PA binding alone is not sufficient to neutralize LT and suggest that for an antibody to effectively block PA-mediated toxicity, it must bind to PA such that one of the requisite toxin functions is disrupted. A vaccine design strategy that directed a higher percentage of the antibody response toward neutralizing epitopes may result in a more efficacious vaccine for the prevention of anthrax infection.

Indexed as

Binding Sites, AntibodyAnimalsAnthrax VaccinesAntibodies, BacterialAntibodies, MonoclonalAntigens, BacterialAntitoxinsBacterial ToxinsCHO CellsCricetinaeCricetulusHumansNeutralization Testsanthrax toxinAnthrax VaccinesAntibodies, BacterialAntibodies, MonoclonalAntigens, BacterialAntitoxinsBacterial Toxins

Identifiers

PMID19223482
PMCPMC2681729
OpenAlexW2125947940

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.