Evidence map›Paper›PMID 24889612›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα.

Kimiko Kuroki, Jing Wang, Toyoyuki Ose, Munechika Yamaguchi, Shigekazu Tabata, Nobuo Maita, Seiko Nakamura, Mizuho Kajikawa, Amane Kogure, Takeshi Satoh and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 13% 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, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Solution NMR Analysis of O-Glycopeptide-Antibody Interaction.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. The mucin-selective protease StcE enables molecular and functional analysis of human cancer-associated mucins.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Precision glycocalyx editing as a strategy for cancer immunotherapy.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. O-glycans direct selectin ligands to lipid rafts on leukocytes.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  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

12 authors at 5 institutions in 1 country.

Kimiko KurokiFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan;
Jing WangDepartment of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan;
Toyoyuki OseFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan;
Munechika YamaguchiMedical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan;
Shigekazu TabataMedical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan;
Nobuo MaitaMedical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan;
Seiko NakamuraMedical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan;
Mizuho KajikawaMedical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan;
Amane KogureDepartment of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan;
Takeshi SatohDepartment of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan;
Hisashi AraseDepartment of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan;Laboratory of Immunochemistry, World Premier International Immunology Frontier Research Center, Osaka University, Osaka 565-0871, Japan; andCore Research for Evolutionary Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan arase@biken.osaka-u.ac.jp maenaka@pharm.hokudai.ac.jp.
Katsumi MaenakaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan;Core Research for Evolutionary Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan arase@biken.osaka-u.ac.jp maenaka@pharm.hokudai.ac.jp.
Kyushu University · JPOsaka University · JPHokkaido University · JPJapan Science and Technology Agency · JPOsaka International University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Paired Ig-like type 2 receptor α (PILRα) recognizes a wide range of O-glycosylated mucin and related proteins to regulate broad immune responses. However, the molecular characteristics of these recognitions are largely unknown. Here we show that sialylated O-linked sugar T antigen (sTn) and its attached peptide region are both required for ligand recognition by PILRα. Furthermore, we determined the crystal structures of PILRα and its complex with an sTn and its attached peptide region. The structures show that PILRα exhibits large conformational change to recognize simultaneously both the sTn O-glycan and the compact peptide structure constrained by proline residues. Binding and functional assays support this binding mode. These findings provide significant insight into the binding motif and molecular mechanism (which is distinct from sugar-recognition receptors) by which O-glycosylated mucin proteins with sTn modifications are recognized in the immune system as well as during viral entry.

Indexed as

Amino Acid SequenceAnimalsCHO CellsCricetinaeCricetulusCrystallography, X-RayGlycosylationHEK293 CellsHumansImmune SystemMembrane GlycoproteinsMiceModels, MolecularMolecular Sequence DataMucinsMutagenesisMembrane GlycoproteinsMucinsPeptidesPILRA protein, humanPolysaccharidesReceptors, ImmunologicRecombinant Fusion Proteinsimmune regulationO-glycosylated proteinpaired receptorX-ray crystallography

Identifiers

PMID24889612
PMCPMC4066494
OpenAlexW2006301332

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.