Evidence map›Paper›PMID 19401597›Full record

ArticleMolecular & cellular proteomics : MCP2009

Surfome analysis as a fast track to vaccine discovery: identification of a novel protective antigen for Group B Streptococcus hypervirulent strain COH1.

Francesco Doro, Sabrina Liberatori, Manuel J Rodríguez-Ortega, Cira D Rinaudo, Roberto Rosini, Marirosa Mora, Maria Scarselli, Emrah Altindis, Romina D'Aurizio, Maria Stella and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
11.1field-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

42 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
  2. Review
  3. Prediction of Potential Drug Targets and Vaccine Candidates Against Antibiotic-ResistantInternational journal of peptide research and therapeutics · 2022
    Article
  4. The S Protein of Group BFrontiers in microbiology · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Surface Structures of Group BMicrobiology spectrum · 2019
    Review
  10. Article
  11. Review
  12. Journal of veterinary science · 2018
    Article
  13. Article
  14. Status of group B streptococcal vaccine development.Clinical and experimental vaccine research · 2018
    Article
  15. Review
  16. Review
  17. Progress toward a group B streptococcal vaccine.Human vaccines & immunotherapeutics · 2018
    Article
  18. Article
  19. Article
  20. Vaccinology: The art of putting together the right ingredients.Human vaccines & immunotherapeutics · 2016
    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

15 authors at 1 institution in 1 country.

Francesco DoroResearch Centre, Novartis Vaccines and Diagnostics, 53100 Siena, Italy.
Sabrina Liberatori
Manuel J Rodríguez-Ortega
Cira D Rinaudo
Roberto Rosini
Marirosa Mora
Maria Scarselli
Emrah Altindis
Romina D'Aurizio
Maria Stella
Immaculada Margarit
Domenico Maione
John L Telford
Nathalie Norais
Guido Grandi
Novartis (Italy) · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Safe recombinant vaccines, based on a small number of antigenic proteins, are emerging as the most attractive, cost-effective solution against infectious diseases. In the present work, we confirmed previous data from our laboratory showing that whole viable bacterial cell treatment with proteases followed by the identification of released peptides by mass spectrometry is the method of choice for the rapid and reliable identification of vaccine candidates in Gram-positive bacteria. When applied to the Group B Streptococcus COH1 strain, 43 surface-associated proteins were identified, including all the protective antigens described in the literature as well as a new protective antigen, the cell wall-anchored protein SAN_1485 belonging to the serine-rich repeat protein family. This strategy overcomes the difficulties so far encountered in the identification of novel vaccine candidates and speeds up the entire vaccine discovery process by reducing the number of recombinant proteins to be tested in the animal model.

Indexed as

Antigens, BacterialStreptococcus agalactiaeVaccines, SyntheticAmino Acid SequenceAnimalsFemaleMolecular Sequence DataProteomeStreptococcal InfectionsAntigens, BacterialProteomeVaccines, Synthetic

Identifiers

PMID19401597
PMCPMC2709197
OpenAlexW2132094784

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.