Evidence map›Paper›PMID 26242409›Full record

ArticleBMC microbiology2015

Fratricide activity of MafB protein of N. meningitidis strain B16B6.

Jesús Arenas, Vincent de Maat, Laura Catón, Massis Krekorian, Juan Cruz Herrero, Flavio Ferrara, Jan Tommassen

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  6. Frontiers in cellular and infection microbiology · 2022
    Review
  7. Editorial: PathogenicFrontiers in cellular and infection microbiology · 2022
    Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Biological Functions of the Secretome ofFrontiers in cellular and infection microbiology · 2017
    Review
  17. 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

7 authors at 1 institution in 1 country.

Jesús ArenasDepartment of Molecular Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands. J.A.arenasbusto@uu.nl.
Vincent de MaatDepartment of Molecular Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands. vincent.de.maat@gmail.com.
Laura CatónDepartment of Molecular Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands. catona.laura@gmail.com.
Massis KrekorianDepartment of Molecular Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands. m.krekorian@students.uu.nl.
Juan Cruz HerreroDepartment of Molecular Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands. j.c.herreromartin@students.uu.nl.
Flavio FerraraDepartment of Molecular Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands. flavio.ferrara88@gmail.com.
Jan TommassenDepartment of Molecular Microbiology, Utrecht University, Padualaan 8, 3584, CH, Utrecht, The Netherlands. J.P.M.Tommassen@uu.nl.
Utrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundNeisseria meningitidis is an inhabitant of the mucosal surfaces of the human nasopharynx. We recently demonstrated that the secreted meningococcal Two-partner secretion protein A (TpsA) is involved in interbacterial competition. The C-terminal end of the large TpsA protein contains a small toxic domain that inhibits the growth of target bacteria. The producing cells are protected from this toxic activity by a small immunity protein that is encoded by the gene immediately downstream of the tpsA gene. Further downstream on the chromosome, a repertoire of toxic modules, designated tpsC cassettes, is encoded that could replace the toxic module of TpsA by recombination. Each tpsC cassette is associated with a gene encoding a cognate immunity protein.

resultsBlast searchers using the toxic domains of TpsA and TpsC proteins as queries identified homologies with the C-terminal part of neisserial MafB proteins, which, for the rest, showed no sequence similarity to TpsA proteins. On the chromosome, mafB genes are part of genomic islands, which include cassettes for additional toxic modules as well as genes putatively encoding immunity proteins. We demonstrate that a MafB protein of strain B16B6 inhibits the growth of a strain that does not produce the corresponding immunity protein. Assays in E. coli confirmed that the C-terminal region of MafB is responsible for toxicity, which is inhibited by the cognate immunity protein. Pull-down assays revealed direct interaction between MafB toxic domains and the cognate immunity proteins.

conclusionsThe meningococcal MafB proteins are novel toxic proteins involved in interbacterial competition.

Indexed as

BacteriocinsDNA, BacterialMafB Transcription FactorMicrobial ViabilityMolecular Sequence DataNeisseria meningitidisSequence Analysis, DNABacteriocinsDNA, BacterialMafB Transcription Factor

Identifiers

PMID26242409
PMCPMC4524018
OpenAlexW1516094891

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.