Evidence map›Paper›PMID 32228455›Full record

ArticleBMC microbiology2020

Vibiro vulnificus hemolysin associates with gangliosides.

Takashige Kashimoto, Hiroyuki Sugiyama, Keigo Kawamidori, Kohei Yamazaki, Takehiro Kado, Kaho Matsuda, Toshio Kodama, Takao Mukai, Shunji Ueno

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Microorganisms · 2025
    Review
  2. Review
  3. Frontiers in immunology · 2020
    Review
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

9 authors at 2 institutions in 1 country.

Takashige KashimotoLaboratory of Veterinary Public Health, School of Veterinary Medicine and Animal Sciences, Kitasato University, Higashi 23-35-1, Towada, Aomori, 034-8628, Japan. kashimot@vmas.kitasato-u.ac.jp.
Hiroyuki SugiyamaLaboratory of Veterinary Public Health, School of Veterinary Medicine and Animal Sciences, Kitasato University, Higashi 23-35-1, Towada, Aomori, 034-8628, Japan.
Keigo KawamidoriLaboratory of Veterinary Public Health, School of Veterinary Medicine and Animal Sciences, Kitasato University, Higashi 23-35-1, Towada, Aomori, 034-8628, Japan.
Kohei YamazakiLaboratory of Veterinary Public Health, School of Veterinary Medicine and Animal Sciences, Kitasato University, Higashi 23-35-1, Towada, Aomori, 034-8628, Japan.
Takehiro KadoLaboratory of Veterinary Public Health, School of Veterinary Medicine and Animal Sciences, Kitasato University, Higashi 23-35-1, Towada, Aomori, 034-8628, Japan.
Kaho MatsudaLaboratory of Veterinary Public Health, School of Veterinary Medicine and Animal Sciences, Kitasato University, Higashi 23-35-1, Towada, Aomori, 034-8628, Japan.
Toshio KodamaDepartment of Bacterial Infections, International Research Center for Infectious Diseases, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan.
Takao MukaiLaboratory of Biomolecular Science, School of Veterinary Medicine and Animal Sciences, Kitasato University, Higashi 23-35-1, Towada, Aomori, Japan.
Shunji UenoLaboratory of Veterinary Public Health, School of Veterinary Medicine and Animal Sciences, Kitasato University, Higashi 23-35-1, Towada, Aomori, 034-8628, Japan.
Kitasato University · JPOsaka University · JP

Funding

Japan Society for the Promotion of Science KAKENHI 18H02350Joint Research Project of the Research Institute for Microbial Diseases, the University of Osaka N/A
6 · The paper itself

Abstract

backgroundVibrio vulnificus hemolysin (VVH) is a pore-forming toxin secreted by Vibrio vulnificus. Cellular cholesterol was believed to be the receptor for VVH, because cholesterol could bind to VVH and preincubation with cholesterol inhibited cytotoxicity. It has been reported that specific glycans such as N-acetyl-D-galactosamine and N-acetyl-D-lactosamine bind to VVH, however, it has not been known whether these glycans could inhibit the cytotoxicity of VVH without oligomer formation. Thus, to date, binding mechanisms of VVH to cellular membrane, including specific receptors have not been elucidated.

resultsWe show here that VVH associates with ganglioside GM1a, Fucosyl-GM1, GD1a, GT1c, and GD1b by glycan array. Among them, GM1a could pulldown VVH. Moreover, the GD1a inhibited the cytotoxicity of VVH without the formation of oligomers.

conclusionThis is the first report of a molecule able to inhibit the binding of VVH to target cells without oligomerization of VVH.

Indexed as

AnimalsBacterial ProteinsBinding SitesCell MembraneCHO CellsCholesterolCricetulusGangliosidesGlycomicsHemolysin ProteinsMicroarray AnalysisProtein BindingProtein ConformationProtein MultimerizationVibrio vulnificusBacterial ProteinsCholesterolGangliosidesHemolysin ProteinsGangliosidesHemolysinReceptorVibrio vulnificus

Identifiers

PMID32228455
PMCPMC7106661
OpenAlexW3013358456

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.