Evidence map›Paper›PMID 28456649›Full record

ArticleMicrobes and infection

The accessory Sec system (SecY2A2) in Streptococcus pneumoniae is involved in export of pneumolysin toxin, adhesion and biofilm formation.

Mikaila Bandara, J Mark Skehel, Aras Kadioglu, Ian Collinson, Angela H Nobbs, Ariel J Blocker, Howard F Jenkinson

Open access · hybridAbstract read
In one paragraph

Article in Microbes and infection. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Microbial biofilm: formation, architecture, antibiotic resistance, and control strategies.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Streptococcus oralis subsp.Infection and immunity · 2019
    Article
  13. Review
  14. Review
  15. Review
  16. Structural basis for the role of serine-rich repeat proteins fromProceedings of the National Academy of Sciences of the United States of America · 2018
    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 4 institutions in 1 country.

Mikaila BandaraSchool of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol, BS1 2LY, UK; School of Cellular & Molecular Medicine, University of Bristol, University Walk, Bristol, BS8 1TD, UK; School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
J Mark SkehelBiological Mass Spectrometry and Proteomics, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Aras KadiogluDepartment of Clinical Infection, Microbiology & Immunology, Institute of Infection and Global Health, University of Liverpool, 8 West Derby Street, Liverpool L69 7BE, UK.
Ian CollinsonSchool of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Angela H NobbsSchool of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol, BS1 2LY, UK.
Ariel J BlockerSchool of Cellular & Molecular Medicine, University of Bristol, University Walk, Bristol, BS8 1TD, UK; School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK. Electronic address: ariel.blocker@bristol.ac.uk.
Howard F JenkinsonSchool of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol, BS1 2LY, UK. Electronic address: howard.jenkinson@bristol.ac.uk.
University Of Bristol Dental Hospital · GBUniversity of Bristol · GBMRC Laboratory of Molecular Biology · GBUniversity of Liverpool · GB

Funding

Medical Research Council 2011-G1001606Medical Research Council MC_U105178788
6 · The paper itself

Abstract

In Streptococcus pneumoniae TIGR4, genes encoding a SecY2A2 accessory Sec system are present within a locus encoding a serine-rich repeat surface protein PsrP. Mutant strains deleted in secA2 or psrP were deficient in biofilm formation, while the ΔsecA2 mutant was reduced in binding to airway epithelial cells. Cell wall protein (CWP) fractions from the ΔsecA2 mutant, but not from the ΔpsrP mutant, were reduced in haemolytic (pneumolysin) activity. Contact-dependent pneumolysin (Ply) activity of wild type TIGR4 cells was ten-fold greater than that of ΔsecA2 mutant cells suggesting that Ply was not active at the ΔsecA2 cell surface. Ply protein was found to be present in the CWP fraction from the ΔsecA2 mutant, but showed aberrant electrophoretic migration indicative of protein modification. Proteomic analyses led to the discovery that the ΔsecA2 mutant CWP fraction was deficient in two glycosidases as well as other enzymes involved in carbohydrate metabolism. Taken collectively the results suggest that positioning of Ply into the cell wall compartment in active form, together with glycosyl hydrolases and adhesins, requires a functional accessory Sec system.

Indexed as

Bacterial AdhesionBacterial ProteinsBacterial Secretion SystemsBiofilmsGene DeletionHumansStreptococcus pneumoniaeStreptolysinsBacterial ProteinsBacterial Secretion SystemsplY protein, Streptococcus pneumoniaeStreptolysinsBiofilmsExportO-glycosidasePneumolysinSecA2Streptococcus pneumoniae

Identifiers

PMID28456649
PMCPMC5526788
OpenAlexW2607697398

What OpenQuestion holds

Textmetadata
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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.