Evidence map›Paper›PMID 31542792›Full record

ArticleHistochemistry and cell biology2019

Nanoscale analysis reveals no domain formation of glycosylphosphatidylinositol-anchored protein SAG1 in the plasma membrane of living Toxoplasma gondii.

Yuna Kurokawa, Tatsunori Masatani, Rikako Konishi, Kanna Tomioku, Xuenan Xuan, Akikazu Fujita

Abstract read
PubMed Publisher
In one paragraph

Article in Histochemistry and cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Zwitterionic Character and Lipid Composition Determine the Behaviour of Glycosylphosphatidylinositol Fragments in Monolayers.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021
    Article
  2. In focus in HCB.Histochemistry and cell biology · 2019
    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

6 authors at 2 institutions in 1 country.

Yuna KurokawaDepartment of Molecular Cell Biology and Biochemistry, Basic Veterinary Medicine, Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan.
Tatsunori MasataniTransboundary Animal Diseases Research Center, Joint Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan.
Rikako KonishiDepartment of Molecular Cell Biology and Biochemistry, Basic Veterinary Medicine, Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan.
Kanna TomiokuDepartment of Molecular Cell Biology and Biochemistry, Basic Veterinary Medicine, Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan.
Xuenan XuanNational Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Inada-cho, Obihiro, 080-8555, Japan.
Akikazu FujitaDepartment of Molecular Cell Biology and Biochemistry, Basic Veterinary Medicine, Faculty of Veterinary Medicine, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan. afujita@vet.kagoshima-u.ac.jp.ORCID http://orcid.org/0000-0002-2990-2134
Kagoshima University · JPObihiro University of Agriculture and Veterinary Medicine · JP

Funding

Japan Society for the Promotion of Science JP16K15056Japan Society for the Promotion of Science JP17H03935
6 · The paper itself

Abstract

Glycosylphosphatidylinositol (GPI)-anchored proteins typically localise to lipid rafts. GPI-anchored protein microdomains may be present in the plasma membrane; however, they have been studied using heterogeneously expressed GPI-anchored proteins, and the two-dimensional distributions of endogenous molecules in the plasma membrane are difficult to determine at the nanometre scale. Here, we used immunoelectron microscopy using a quick-freezing and freeze-fracture labelling (QF-FRL) method to examine the distribution of the endogenous GPI-anchored protein SAG1 in Toxoplasma gondii at the nanoscale. QF-FRL physically immobilised molecules in situ, minimising the possibility of artefactual perturbation. SAG1 labelling was observed in the exoplasmic, but not cytoplasmic, leaflets of T. gondii plasma membrane, whereas none was detected in any leaflet of the inner membrane complex. Point pattern analysis of SAG1 immunogold labelling revealed mostly random distribution in T. gondii plasma membrane. The present method obtains information on the molecular distribution of natively expressed GPI-anchored proteins and demonstrates that SAG1 in T. gondii does not form significant microdomains in the plasma membrane.

Indexed as

AnimalsAntigens, ProtozoanCell MembraneFibroblastsGlycosylphosphatidylinositolsHumansMiceMicroscopy, ImmunoelectronProtozoan ProteinsToxoplasmaAntigens, ProtozoanGlycosylphosphatidylinositolsProtozoan ProteinsSAG1 antigen, ToxoplasmaElectron microscopyFreeze-fractureGPI-anchored proteinLaftLipid

Identifiers

PMID31542792
OpenAlexW2974419033

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.