Evidence map›Paper›PMID 23396847›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Defining a protective epitope on factor H binding protein, a key meningococcal virulence factor and vaccine antigen.

Enrico Malito, Agnese Faleri, Paola Lo Surdo, Daniele Veggi, Giulietta Maruggi, Eva Grassi, Elena Cartocci, Isabella Bertoldi, Alessia Genovese, Laura Santini and 17 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
11.8field-weighted citation impact, top 1% 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

77 citing papers in PubMed, 132 citations in OpenAlex.

  1. Article
  2. Article
  3. Discovery and characterization of an anti-Frontiers in microbiology · 2026
    Article
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  5. Review
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  7. Multi-perspectives and challenges in identifying B-cell epitopes.Protein science : a publication of the Protein Society · 2023
    Review
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17 more citing papers are in PubMed but not listed here.

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

27 authors at 5 institutions in 3 countries.

Enrico MalitoResearch Center, Novartis Vaccines and Diagnostics srl, 53100 Siena, Italy.
Agnese Faleri
Paola Lo Surdo
Daniele Veggi
Giulietta Maruggi
Eva Grassi
Elena Cartocci
Isabella Bertoldi
Alessia Genovese
Laura Santini
Giacomo Romagnoli
Erica Borgogni
Sébastien Brier
Carla Lo Passo
Maria Domina
Flora Castellino
Franco Felici
Stijn van der Veen
Steven Johnson
Susan M Lea
Christoph M Tang
Mariagrazia Pizza
Silvana Savino
Nathalie Norais
Rino Rappuoli
Matthew J Bottomley
Vega Masignani
Novartis (Italy) · ITNovartis (Switzerland) · CHUniversity of Oxford · GBUniversity of Messina · ITUniversity of Molise · IT

Funding

Medical Research CouncilWellcome Trust
6 · The paper itself

Abstract

Mapping of epitopes recognized by functional monoclonal antibodies (mAbs) is essential for understanding the nature of immune responses and designing improved vaccines, therapeutics, and diagnostics. In recent years, identification of B-cell epitopes targeted by neutralizing antibodies has facilitated the design of peptide-based vaccines against highly variable pathogens like HIV, respiratory syncytial virus, and Helicobacter pylori; however, none of these products has yet progressed into clinical stages. Linear epitopes identified by conventional mapping techniques only partially reflect the immunogenic properties of the epitope in its natural conformation, thus limiting the success of this approach. To investigate antigen-antibody interactions and assess the potential of the most common epitope mapping techniques, we generated a series of mAbs against factor H binding protein (fHbp), a key virulence factor and vaccine antigen of Neisseria meningitidis. The interaction of fHbp with the bactericidal mAb 12C1 was studied by various epitope mapping methods. Although a 12-residue epitope in the C terminus of fHbp was identified by both Peptide Scanning and Phage Display Library screening, other approaches, such as hydrogen/deuterium exchange mass spectrometry (MS) and X-ray crystallography, showed that mAb 12C1 occupies an area of ∼1,000 Å(2) on fHbp, including >20 fHbp residues distributed on both N- and C-terminal domains. Collectively, these data show that linear epitope mapping techniques provide useful but incomplete descriptions of B-cell epitopes, indicating that increased efforts to fully characterize antigen-antibody interfaces are required to understand and design effective immunogens.

Indexed as

Antibodies, MonoclonalAntibody SpecificityAntigens, BacterialBacterial ProteinsCell Surface Display TechniquesCrystallography, X-RayDeuterium Exchange MeasurementEpitope MappingEpitopesMass SpectrometryMeningococcal InfectionsMeningococcal VaccinesModels, MolecularNeisseria meningitidisPeptidesProtein BindingAntibodies, MonoclonalAntigens, BacterialBacterial ProteinsEpitopesfactor H-binding protein, Neisseria meningitidisMeningococcal VaccinesPeptidesVirulence Factors

Identifiers

PMID23396847
PMCPMC3587270
OpenAlexW2012763858

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.