Evidence map›Paper›PMID 28848046›Full record

ArticleThe Journal of biological chemistry2017

Dectin-1 intracellular domain determines species-specific ligand spectrum by modulating receptor sensitivity.

Tomotsugu Takano, Chihiro Motozono, Takashi Imai, Koh-Hei Sonoda, Yoichi Nakanishi, Sho Yamasaki

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Review
  8. Article
  9. Self-recognition through Dectin-1 exacerbates liver inflammation.Genes to cells : devoted to molecular & cellular mechanisms · 2024
    Article
  10. Preparation ofACS applied bio materials · 2023
    Article
  11. Frontiers in nutrition · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Interaction Between Dendritic Cells andFrontiers in cellular and infection microbiology · 2020
    Article
  16. Article
  17. Lipoteichoic acid anchor triggers Mincle to drive protective immunity against invasive group AProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. 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

6 authors at 3 institutions in 3 countries.

Tomotsugu TakanoFrom the Division of Molecular Immunology, Medical Institute of Bioregulation.
Chihiro Motozonothe Department of Molecular Immunology, Research Institute for Microbial Diseases, and motozono@biken.osaka-u.ac.jp.
Takashi ImaiFrom the Division of Molecular Immunology, Medical Institute of Bioregulation.
Koh-Hei SonodaDepartment of Ocular Pathology and Imaging Science, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582.
Yoichi NakanishiResearch Institute for Diseases of the Chest, Graduate School of Medical Sciences, and.
Sho YamasakiFrom the Division of Molecular Immunology, Medical Institute of Bioregulation, yamasaki@biken.osaka-u.ac.jp.
Kyushu University · JPSt. Petersburg Institute of Bioregulation and Gerontology · RUChiba University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

C-type lectin receptors (CLRs) comprise a large family of immunoreceptors that recognize polysaccharide ligands exposed on pathogen surfaces and are conserved among mammals. However, interspecies differences in their ligand spectrums are not fully understood. Dectin-1 is a well-characterized CLR that recognizes β-glucan. We report here that seaweed-derived fucan activates cells expressing human Dectin-1 but not mouse Dectin-1. Low-valency β-glucan components within fucan appeared to be responsible for this activation, as the ligand activity was eliminated by β-glucanase treatment. The low-valency β-glucan laminarin also acted as an agonist for human Dectin-1 but not for mouse Dectin-1, whereas the high-valency β-glucan curdlan activated both human and mouse Dectin-1. Reciprocal mutagenesis analysis revealed that the ligand-binding domain of human Dectin-1 does not determine its unique sensitivity to low-valency β-glucan. Rather, we found that its intracellular domain renders human Dectin-1 reactive to low-valency β-glucan ligand. Substitution with two amino acids, Glu

Indexed as

Amino Acid SubstitutionAnimalsbeta-GlucansCell LineDectin-1GlucansHumansLectins, C-TypeMiceMutagenesisMutation, MissensePolysaccharidesProtein DomainsSpecies SpecificitySubstrate Specificitybeta-GlucansCLEC7A protein, humancurdlanDectin-1fucoidanGlucanslaminaranLectins, C-TypePolysaccharidesglucanimmunologylectinpolysaccharidereceptorsignal transduction

Identifiers

PMID28848046
PMCPMC5641891
OpenAlexW2747690592

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.