Evidence map›Paper›PMID 19948796›Full record

ArticleJournal of bacteriology2010

Expression of factor H binding protein of meningococcus responds to oxygen limitation through a dedicated FNR-regulated promoter.

Francesca Oriente, Vincenzo Scarlato, Isabel Delany

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The Host-Pathogen Interactions and Epicellular Lifestyle ofFrontiers in cellular and infection microbiology · 2022
    Review
  5. Article
  6. Article
  7. Article
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  9. Article
  10. Article
  11. Review
  12. Biological Functions of the Secretome ofFrontiers in cellular and infection microbiology · 2017
    Review
  13. Article
  14. Expression of factor H binding protein in meningococcal strains can vary at least 15-fold and is genetically determined.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Review
  16. Vaccines, reverse vaccinology, and bacterial pathogenesis.Cold Spring Harbor perspectives in medicine · 2013
    Article
  17. Article
  18. Review
  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

3 authors at 1 institution in 1 country.

Francesca OrienteNovartis Vaccines, Microbial Molecular Biology, 53100 Siena, Italy.
Vincenzo Scarlato
Isabel Delany
Novartis (Italy) · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Factor H binding protein (fHBP) is a surface-exposed lipoprotein in Neisseria meningitidis, which is a component of several investigational vaccines against serogroup B meningococcus (MenB) currently in development. fHBP enables the bacterium to evade complement-mediated killing by binding factor H, a key downregulator of the complement alternative pathway, and, in addition, fHBP is important for meningococcal survival in the presence of the antimicrobial peptide LL-37. In this study, we investigate the molecular mechanisms involved in transcription and regulation of the fHBP-encoding gene, fhbp. We show that the fHBP protein is expressed from two independent transcripts: one bicistronic transcript that includes the upstream gene and a second shorter monocistronic transcript from its own dedicated promoter, P(fhbp). Transcription from the promoter P(fhbp) responds to oxygen limitation in an FNR-dependent manner, and, accordingly, the FNR protein binds to a P(fhbp) probe in vitro. Furthermore, expression in meningococci of a constitutively active FNR mutant results in the overexpression of the fHBP protein. Finally, the analysis of fHBP regulation was extended to a panel of strains expressing different fHBP allelic variants at different levels, and we demonstrate that FNR is involved in the regulation of this antigen in all but one of the strains tested. Our data suggest that oxygen limitation may play an important role in inducing the expression of fHBP from a dedicated FNR-regulated promoter. This implies a role for this protein in microenvironments lacking oxygen, for instance in the submucosa or intracellularly, in addition to its demonstrated role in serum resistance in the blood.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsBase SequenceBlotting, NorthernBlotting, WesternDeoxyribonuclease IDNA FootprintingModels, GeneticMolecular Sequence DataNeisseria meningitidisOxygenPromoter Regions, GeneticProtein BindingReverse Transcriptase Polymerase Chain ReactionBacterial ProteinsDeoxyribonuclease IOxygen

Identifiers

PMID19948796
PMCPMC2812459
OpenAlexW2158338880

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.