Evidence map›Paper›PMID 19617628›Full record

ArticleThe Journal of biological chemistry2009

Identification of linear epitopes in Bacillus anthracis protective antigen bound by neutralizing antibodies.

Nareen Abboud, Magdia De Jesus, Antonio Nakouzi, Radames J B Cordero, Mario Pujato, András Fiser, Johanna Rivera, Arturo Casadevall

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

29 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Recombinant full-lengthFrontiers in immunology · 2022
    Article
  3. Article
  4. Article
  5. Design of a Multi-epitope Vaccine AgainstInternational journal of peptide research and therapeutics · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Molecular determinants for a cardiovascular collapse in anthrax.Frontiers in bioscience (Elite edition) · 2014
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
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

8 authors at 2 institutions in 1 country.

Nareen AbboudDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Magdia De Jesus
Antonio Nakouzi
Radames J B Cordero
Mario Pujato
András Fiser
Johanna Rivera
Arturo Casadevall
Albert Einstein College of Medicine · USOffice of Infectious Diseases · US

Funding

Viral Pathogenesis and TherapeuticsU54AI057158 · NIAID · WADSWORTH CENTER · PI LIPKIN, W. IAN · 2003 to 2014
$100.8M
NIAID NIH HHS 2U54AI057158-06NIAID NIH HHS U54 AI057158
6 · The paper itself

Abstract

Protective antigen (PA), the binding subunit of anthrax toxin, is the major component in the current anthrax vaccine, but the fine antigenic structure of PA is not well defined. To identify linear neutralizing epitopes of PA, 145 overlapping peptides covering the entire sequence of the protein were synthesized. Six monoclonal antibodies (mAbs) and antisera from mice specific for PA were tested for their reactivity to the peptides by enzyme-linked immunosorbent assays. Three major linear immunodominant B-cell epitopes were mapped to residues Leu(156) to Ser(170), Val(196) to Ile(210), and Ser(312) to Asn(326) of the PA protein. Two mAbs with toxin-neutralizing activity recognized two different epitopes in close proximity to the furin cleavage site in domain 1. The three-dimensional complex structure of PA and its neutralizing mAbs 7.5G and 19D9 were modeled using the molecular docking method providing models for the interacting epitope and paratope residues. For both mAbs, LeTx neutralization was associated with interference with furin cleavage, but they differed in effectiveness depending on whether they bound on the N- or C-terminal aspect of the cleaved products. The two peptides containing these epitopes that include amino acids Leu(156)-Ser(170) and Val(196)-Ile(210) were immunogenic and elicited neutralizing antibody responses to PA. These results identify the first linear neutralizing epitopes of PA and show that peptides containing epitope sequences can elicit neutralizing antibody responses, a finding that could be exploited for vaccine design.

Indexed as

AnimalsAntibodiesAntigens, BacterialBacillus anthracisBacterial ToxinsB-LymphocytesEnzyme-Linked Immunosorbent AssayEpitope MappingEpitopesFemaleHybridomasMacrophagesMiceMice, Inbred BALB CMolecular Sequence DataNeutralization Testsanthrax toxinAntibodiesAntigens, BacterialBacterial ToxinsEpitopes

Identifiers

PMID19617628
PMCPMC2757211
OpenAlexW2111944535

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.