Evidence map›Paper›PMID 25919894›Full record

ArticleChembiochem : a European journal of chemical biology2015

Defining the Interaction of Human Soluble Lectin ZG16p and Mycobacterial Phosphatidylinositol Mannosides.

Shinya Hanashima, Sebastian Götze, Yan Liu, Akemi Ikeda, Kyoko Kojima-Aikawa, Naoyuki Taniguchi, Daniel Varón Silva, Ten Feizi, Peter H Seeberger, Yoshiki Yamaguchi

Open access · greenAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. NMR of Gangliosides.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Microbe-focused glycan array screening platform.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Review
  9. Article
  10. Recognition of microbial glycans by soluble human lectins.Current opinion in structural biology · 2017
    Review
  11. Review
  12. Biophysical Analyses for Probing Glycan-Protein Interactions.Advances in experimental medicine and biology
    Review
  13. 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

10 authors at 5 institutions in 3 countries.

Shinya HanashimaStructural Glycobiology Team, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, RIKEN Global Research Cluster, Wako, Saitama 351-0198 (Japan).
Sebastian GötzeDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14424 Potsdam (Germany).
Yan LiuGlycosciences Laboratory, Department of Medicine, Imperial College London, Du Cane Road, London W12 0NN (UK).
Akemi IkedaStructural Glycobiology Team, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, RIKEN Global Research Cluster, Wako, Saitama 351-0198 (Japan).
Kyoko Kojima-AikawaThe Glycoscience Institute, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112-8610 (Japan).
Naoyuki TaniguchiDisease Glycomics Team, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, RIKEN Global Research Cluster, Wako, Saitama 351-0198 (Japan).
Daniel Varón SilvaDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14424 Potsdam (Germany).
Ten FeiziGlycosciences Laboratory, Department of Medicine, Imperial College London, Du Cane Road, London W12 0NN (UK).
Peter H SeebergerDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14424 Potsdam (Germany).
Yoshiki YamaguchiStructural Glycobiology Team, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, RIKEN Global Research Cluster, Wako, Saitama 351-0198 (Japan). yyoshiki@riken.jp.
RIKEN · JPFreie Universität Berlin · DEImperial College London · GBMax Planck Institute of Colloids and Interfaces · DEOtsuka (Japan) · JP

Funding

Wellcome TrustWellcome Trust WT093378MAWellcome Trust WT099197MA
6 · The paper itself

Abstract

ZG16p is a soluble mammalian lectin that interacts with mannose and heparan sulfate. Here we describe detailed analysis of the interaction of human ZG16p with mycobacterial phosphatidylinositol mannosides (PIMs) by glycan microarray and NMR. Pathogen-related glycan microarray analysis identified phosphatidylinositol mono- and di-mannosides (PIM1 and PIM2) as novel ligand candidates of ZG16p. Saturation transfer difference (STD) NMR and transferred NOE experiments with chemically synthesized PIM glycans indicate that PIMs preferentially interact with ZG16p by using the mannose residues. The binding site of PIM was identified by chemical-shift perturbation experiments with uniformly (15)N-labeled ZG16p. NMR results with docking simulations suggest a binding mode of ZG16p and PIM glycan; this will help to elucidate the physiological role of ZG16p.

Indexed as

Carbohydrate SequenceHost-Pathogen InteractionsHumansLectinsMolecular Docking SimulationMolecular Sequence DataMycobacteriumMycobacterium InfectionsPhosphatidylinositolsProtein BindingLectinsphosphatidylinositol mannosidePhosphatidylinositolsZG16 protein, humancarbohydrate microarrayschemical synthesislectinsmicroarraysNMR spectroscopyphosphatidyl inositol mannoside

Identifiers

PMID25919894
PMCPMC5896728
OpenAlexW2022872865

What OpenQuestion holds

Textmetadata
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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.