Evidence map›Paper›PMID 22847002›Full record

ArticleThe Journal of biological chemistry2012

Clostridium perfringens alpha-toxin recognizes the GM1a-TrkA complex.

Masataka Oda, Michiko Kabura, Teruhisa Takagishi, Ayaka Suzue, Kaori Tominaga, Shiori Urano, Masahiro Nagahama, Keiko Kobayashi, Keiko Furukawa, Koichi Furukawa and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 43 citations in OpenAlex.

  1. Epidemiological and Metabolic Characteristics ofAnimals : an open access journal from MDPI · 2026
    Article
  2. Unveiling the pathogenic mechanisms ofEmerging microbes & infections · 2024
    Review
  3. Preparation and Application ofVeterinary sciences · 2024
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Histotoxic Clostridial Infections.Microbiology spectrum · 2019
    Article
  10. Communications biology · 2019
    Article
  11. Review
  12. Protein Toxins That Utilize Gangliosides as Host Receptors.Progress in molecular biology and translational science · 2018
    Review
  13. Article
  14. Article
  15. Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  16. Review
  17. Article
  18. Article
  19. Gas-Forming Pyogenic Liver Abscess with Septic Shock.Case reports in critical care · 2015
    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

11 authors at 2 institutions in 1 country.

Masataka OdaDepartment of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Yamashiro-cho, Tokushima 770-8514, Japan. masa@ph.bunri-u.ac.jp
Michiko Kabura
Teruhisa Takagishi
Ayaka Suzue
Kaori Tominaga
Shiori Urano
Masahiro Nagahama
Keiko Kobayashi
Keiko Furukawa
Koichi Furukawa
Jun Sakurai
Tokushima Bunri University · JPNagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clostridium perfringens alpha-toxin is the major virulence factor in the pathogenesis of gas gangrene. Alpha-toxin is a 43-kDa protein with two structural domains; the N-domain contains the catalytic site and coordinates the divalent metal ions, and the C-domain is a membrane-binding site. The role of the exposed loop region (72-93 residues) in the N-domain, however, has been unclear. Here we show that this loop contains a ganglioside binding motif (H … SXWY … G) that is the same motif seen in botulinum neurotoxin and directly binds to a specific conformation of the ganglioside Neu5Acα2-3(Galβ1-3GalNAcβ1-4)Galβ1-4Glcβ1Cer (GM1a) through a carbohydrate moiety. Confocal microscopy analysis using fluorescently labeled BODIPY-GM1a revealed that the toxin colocalized with GM1a and induced clustering of GM1a on the cell membranes. Alpha-toxin was only slightly toxic in β1,4-N-acetylgalactosaminyltransferase knock-out mice, which lack the a-series gangliosides that contain GM1a, but was highly toxic in α2,8-sialyltransferase knock-out mice, which lack both b-series and c-series gangliosides, similar to the control mice. Moreover, experiments with site-directed mutants indicated that Trp-84 and Tyr-85 in the exposed alpha-toxin loop play an important role in the interaction with GM1a and subsequent activation of TrkA. These results suggest that binding of alpha-toxin to GM1a facilitates the activation of the TrkA receptor and induces a signal transduction cascade that promotes the release of chemokines. Therefore, we conclude that GM1a is the primary cellular receptor for alpha-toxin, which can be a potential target for drug developed against this pathogen.

Indexed as

Clostridium perfringensAmino Acid MotifsAmino Acid SubstitutionAnimalsBacterial Toxinsbeta-D-Galactoside alpha 2-6-SialyltransferaseCalcium-Binding ProteinsCell LineChemokinesG(M1) GangliosideMacrophages, PeritonealMiceMice, KnockoutMutagenesis, Site-DirectedN-AcetylgalactosaminyltransferasesProtein Structure, Tertiaryalpha toxin, Clostridium perfringensBacterial Toxinsbeta-D-Galactoside alpha 2-6-SialyltransferaseCalcium-Binding ProteinsChemokinesganglioside GM1alphaG(M1) GangliosideN-Acetylgalactosaminyltransferases(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferaseReceptor, trkASialyltransferasesType C Phospholipases

Identifiers

PMID22847002
PMCPMC3463319
OpenAlexW2142769627

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.