Evidence map›Paper›PMID 21422174›Full record

ArticleInfection and immunity2011

Deletion of a cation transporter promotes lysis in Streptococcus pneumoniae.

Jolanda Neef, Vahid Farshchi Andisi, Kwang S Kim, Oscar P Kuipers, Jetta J E Bijlsma

Abstract read
In one paragraph

Article in Infection and immunity, 2011. 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
–field-weighted citation impact
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.

  1. Fluoride triggers lysis inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. P-type ATPase magnesium transporter MgtA acts as a dimer.Nature structural & molecular biology · 2025
    Article
  3. Article
  4. The bacterial tyrosine kinase system CpsBCD governs the length of capsule polymers.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. TheApplied and environmental microbiology · 2020
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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

5 authors.

Jolanda NeefDepartment of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Rijksuniversiteit Groningen, Nijenborgh 7, 9747 AG Groningen, Netherlands.
Vahid Farshchi Andisi
Kwang S Kim
Oscar P Kuipers
Jetta J E Bijlsma

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus pneumoniae is a significant human pathogen which causes respiratory and serious invasive diseases. Mg(2+) is essential for life, and its concentration varies throughout the human body. Magnesium uptake plays an important role in the virulence of many bacterial pathogens. To study the Mg(2+) uptake of S. pneumoniae strain D39, a mutant was generated in SPD1383, a P-type ATPase with homology to the Salmonella Mg(2+) transporter MgtA, which has also been shown to be a Ca(2+) exporter in strain TIGR4. Under low-Ca(2+) conditions, mutation led to a growth defect in complex medium and the gene was nearly essential for growth under low-Mg(2+) conditions. Addition of Mg(2+) restored the normal growth of the mutant in all cases, but the addition of other divalent cations had no effect. Addition of Ca(2+), Mn(2+), and Zn(2+) in the presence of high Mg(2+) concentrations inhibited restoration of growth. The mutant was unable to proliferate in blood, which was also alleviated by the addition of Mg(2+). The protein was located in the membrane and produced in various S. pneumoniae strains and pathogenic streptococcal species. Surprisingly, mutation of the gene led to an elevated toxicity for endothelial cells. This was caused by an increased amount of pneumolysin in the medium, mediated by elevated lysis of the mutant. Thus, in this study, we uncovered a role for SPD1383 in Mg(2+) uptake and hypothesize that the protein is a Mg(2+/)Ca(2+) antiporter. Furthermore, a disturbance in Mg(2+) homeostasis seems to promote lysis of S. pneumoniae.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsBlotting, WesternCalciumCalcium-Transporting ATPasesCell LineEndothelial CellsHumansMagnesiumMembrane Transport ProteinsOligonucleotide Array Sequence AnalysisSequence DeletionStreptococcus pneumoniaeStreptolysinsZincAdenosine TriphosphatasesBacterial ProteinsCalciumCalcium-Transporting ATPasesMagnesiumMembrane Transport ProteinsMgtA protein, bacteriaplY protein, Streptococcus pneumoniaeStreptolysinsZinc

Identifiers

PMID21422174
PMCPMC3125841

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.