Evidence map›Paper›PMID 26059530›Full record

ArticleMolecular microbiology2015

Dual modes of membrane binding direct pore formation by Streptolysin O.

Cara C Mozola, Michael G Caparon

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
3.0field-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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Microorganisms · 2022
    Article
  6. Article
  7. Structure of the Streptococcus pyogenes NADJournal of bacteriology · 2022
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. The tuberculosis necrotizing toxin is an NADThe Journal of biological chemistry · 2019
    Article
  14. Group AFrontiers in cellular and infection microbiology · 2019
    Article
  15. Article
  16. Binding of NADmBio · 2017
    Article
  17. Article
  18. Review
  19. 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

2 authors at 1 institution in 1 country.

Cara C MozolaDepartment of Molecular Microbiology, Washington University School of Medicine, Saint Louis, MO, 63110-1093, USA.
Michael G CaparonDepartment of Molecular Microbiology, Washington University School of Medicine, Saint Louis, MO, 63110-1093, USA.
Washington University in St. Louis · US

Funding

Cytolysin-mediated translocation in S.pyogenes virulenceR01AI064721 · NIAID · WASHINGTON UNIVERSITY · PI CAPARON, MICHAEL G. · 2005 to 2014
$3.3M
NIAID NIH HHS AI064721NIAID NIH HHS R01 AI064721
6 · The paper itself

Abstract

Effector translocation is central to the virulence of many bacterial pathogens, including Streptococcus pyogenes, which utilizes the cholesterol-dependent cytolysin Streptolysin O (SLO) to translocate the NAD(+) glycohydrolase SPN into host cells during infection. SLO's translocation activity does not require host cell membrane cholesterol or pore formation by SLO, yet SLO does form pores during infection via a cholesterol-dependent mechanism. Although cholesterol was considered the primary receptor for SLO, SLO's membrane-binding domain also encodes a putative carbohydrate-binding site, implicating a potential glycan receptor in binding and pore formation. Analysis of carbohydrate-binding site SLO mutants and carbohydrate-defective cell lines revealed that glycan recognition is involved in SLO's pore formation pathway and is an essential step when SLO is secreted by non-adherent bacteria, as occurs during lysis of erythrocytes. However, SLO also recognizes host cell membranes via a second mechanism when secreted from adherent bacteria, which requires co-secretion of SPN but not glycan binding by SLO. This SPN-mediated membrane binding of SLO correlates with SPN translocation, and requires SPN's non-enzymatic domain, which is predicted to adopt the structure of a carbohydrate-binding module. SPN-dependent membrane binding also promotes pore formation by SLO, demonstrating that pore formation can occur by distinct pathways during infection.

Indexed as

AnimalsBacterial InfectionsBacterial ProteinsCarbohydrate MetabolismCell MembraneCHO CellsCholesterolCricetulusEscherichia coliHemolysisMutationNAD+ NucleosidaseProtein BindingProtein TransportStreptococcus pyogenesStreptolysinsBacterial ProteinsCholesterolNAD+ Nucleosidasestreptolysin OStreptolysins

Identifiers

PMID26059530
PMCPMC4692278
OpenAlexW2160235961

What OpenQuestion holds

Textmetadata
LicenceTDM
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.