Evidence map›Paper›PMID 21847558›Full record

ArticlePflugers Archiv : European journal of physiology2011

Haemolysis induced by α-toxin from Staphylococcus aureus requires P2X receptor activation.

Marianne Skals, Jens Leipziger, Helle A Praetorius

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.6field-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

31 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. P2RX7 at the Host-Pathogen Interface of Infectious Diseases.Microbiology and molecular biology reviews : MMBR · 2021
    Review
  6. Article
  7. Review
  8. Article
  9. Mechanisms protecting host cells against bacterial pore-forming toxins.Cellular and molecular life sciences : CMLS · 2019
    Review
  10. Erythrocyte P2XCritical care (London, England) · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. P2XFrontiers in cellular and infection microbiology · 2017
    Article
  17. Article
  18. Article
  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.

Marianne SkalsDepartment of Biomedicine, Aarhus University, Ole Worms Allé 4, build. 1160, 8000, Aarhus C, Denmark.
Jens Leipziger
Helle A Praetorius
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recently, it was documented that α-haemolysin (HlyA) from Escherichia coli uses erythrocyte P2 receptors cause lysis. This finding was surprising as it appeared firmly established that HlyA-dependent pore formation per se is sufficient for full cell lysis. We discovered that HlyA induced a sequential process of shrinkage and swelling and that the final haemolysis is completely prevented by blockers of P2X receptors and pannexin channels. This finding has potential clinical relevance as it may offer specific pharmacological interference to ameliorate haemolysis inflicted by pore-forming bacterial toxins. In this context, it is essential to know whether this is specific to HlyA-induced cell damage or if other bacterial pore-forming toxins involve purinergic signals to orchestrate haemolysis. Here, we investigate if the haemolysis produced by α-toxin from Staphylococcus aureus involves P2 receptor activation. We observed that α-toxin-induced haemolysis is completely blocked by the unselective P2 receptor antagonist pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid. Moreover, several selective blockers of P2X(1) and P2X(7) ionotropic receptors abolished haemolysis in murine and equine erythrocytes. Inhibitors of pannexin channels partially reduced the α-toxin induced lysis. Thus, we conclude that α-toxin, similar to HlyA from E. coli produces cell damage by specific activation of a purinergic signalling cascade. These data indicate that pore-forming toxins in general require purinergic signalling to elicit their toxicity.

Indexed as

AnimalsBacterial ToxinsCarbenoxoloneConnexinsEscherichia coli ProteinsFemaleHemolysin ProteinsHemolysisHorsesHumansMaleMiceNerve Tissue ProteinsPyridoxal PhosphateReceptors, Purinergic P2XReceptors, Purinergic P2X7Bacterial ToxinsCarbenoxoloneConnexinsEscherichia coli ProteinsHemolysin ProteinsHlya protein, E coliNerve Tissue ProteinsPanx1 protein, mousePyridoxal Phosphatepyridoxal phosphate-6-azophenyl-2',4'-disulfonic acidReceptors, Purinergic P2XReceptors, Purinergic P2X7staphylococcal alpha-toxin

Identifiers

PMID21847558
OpenAlexW1977112623

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.