Evidence map›Paper›PMID 27808110›Full record

ArticleScientific reports2016

Structural characterisation of high affinity Siglec-2 (CD22) ligands in complex with whole Burkitt's lymphoma (BL) Daudi cells by NMR spectroscopy.

Paul D Madge, Andrea Maggioni, Mauro Pascolutti, Moein Amin, Mario Waespy, Bernadette Bellette, Robin J Thomson, Sørge Kelm, Mark von Itzstein, Thomas Haselhorst

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

  1. Methods for Investigating Siglec-Ganglioside Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Article
  3. Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Glycan structures and their interactions with proteins. A NMR view.Current opinion in structural biology · 2020
    Review
  9. Article
  10. 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

10 authors at 2 institutions in 2 countries.

Paul D MadgeInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Andrea MaggioniInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Mauro PascoluttiInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Moein AminInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Mario WaespyCentre for Biomolecular Interactions Bremen, Department of Biology and Chemistry, University of Bremen, 28334 Bremen, Germany.
Bernadette BelletteInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Robin J ThomsonInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Sørge KelmInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Mark von ItzsteinInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Thomas HaselhorstInstitute for Glycomics, Gold Coast Campus, Griffith University, Queensland, 4222, Australia.
Griffith University · AUUniversity of Bremen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Siglec-2 undergoes constitutive endocytosis and is a drug target for autoimmune diseases and B cell-derived malignancies, including hairy cell leukaemia, marginal zone lymphoma, chronic lymphocytic leukaemia and non-Hodgkin's lymphoma (NHL). An alternative to current antibody-based therapies is the use of liposomal nanoparticles loaded with cytotoxic drugs and decorated with Siglec-2 ligands. We have recently designed the first Siglec-2 ligands (9-biphenylcarboxamido-4-meta-nitrophenyl-carboxamido-Neu5Acα2Me, 9-BPC-4-mNPC-Neu5Acα2Me) with simultaneous modifications at C-4 and C-9 position. In the current study we have used Saturation Transfer Difference (STD) NMR spectroscopy to monitor the binding of 9-BPC-4-mNPC-Neu5Acα2Me to Siglec-2 present on intact Burkitt's lymphoma Daudi cells. Pre-treatment of cells with periodate resulted in significantly higher STD NMR signal intensities for 9-BPC-4-mNPC-Neu5Acα2Me as the cells were more susceptible to ligand binding because cis-binding on the cell surface was removed. Quantification of STD NMR effects led to a cell-derived binding epitope of 9-BPC-4-mNPC-Neu5Acα2Me that facilitated the design and synthesis of C-2, C-3, C-4 and C-9 tetra-substituted Siglec-2 ligands showing an 88-fold higher affinity compared to 9-BPC-Neu5Acα2Me. This is the first time a NMR-based binding study of high affinity Siglec-2 (CD22) ligands in complex with whole Burkitt's lymphoma Daudi cells has been described that might open new avenues in developing tailored therapeutics and personalised medicine.

Indexed as

Magnetic Resonance SpectroscopyBurkitt LymphomaCell Line, TumorEpitopesFlow CytometryHEK293 CellsHumansLigandsN-Acetylneuraminic AcidPeriodic AcidRecombinant ProteinsSialic Acid Binding Ig-like Lectin 2Surface Plasmon ResonanceTransfectionEpitopesLigandsmetaperiodateN-Acetylneuraminic AcidPeriodic AcidRecombinant ProteinsSialic Acid Binding Ig-like Lectin 2

Identifiers

PMID27808110
PMCPMC5093622
OpenAlexW2548144941

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.