Evidence map›Paper›PMID 37087495›Full record

ArticleNature communications2023

Siglec-6 mediates the uptake of extracellular vesicles through a noncanonical glycolipid binding pocket.

Edward N Schmidt, Dimitra Lamprinaki, Kelli A McCord, Maju Joe, Mirat Sojitra, Ayk Waldow, Jasmine Nguyen, John Monyror, Elena N Kitova, Fahima Mozaneh and 17 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Methods for Investigating Siglec-Ganglioside Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  11. Siglecs: From Biomodulation to Immunotherapy.Current protein & peptide science · 2026
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

27 authors at 1 institution in 2 countries.

Edward N SchmidtDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Dimitra LamprinakiDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Kelli A McCordDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0001-6833-1509
Maju JoeDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0003-0664-5275
Mirat SojitraDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0002-7660-5490
Ayk WaldowDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Jasmine NguyenDepartment of Obstetrics & Gynaecology and Physiology University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0003-0712-6987
John MonyrorDepartment of Pharmacology, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0002-6909-9147
Elena N KitovaDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0003-0812-3286
Fahima MozanehDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Xue Yan GuoDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Jaesoo JungDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Jhon R EnterinaDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB, Canada.
Gour C DaskhanDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Ling HanDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Amanda R KryslerDepartment of Pharmacology, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0001-5549-0287
Christopher R CromwellDepartment of Pharmacology, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0001-5147-1441
Basil P HubbardDepartment of Pharmacology, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0003-4353-9674
Lori J WestDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0002-1990-3651
Marianne KulkaDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0003-4741-9290
Simonetta SipioneDepartment of Pharmacology, University of Alberta, Edmonton, AB, Canada.
John S KlassenDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.
Ratmir DerdaDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0003-1365-6570
Todd L LowaryDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0002-8331-8211
Lara K MahalDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0003-4791-8524
Meghan R RiddellDepartment of Obstetrics & Gynaecology and Physiology University of Alberta, Edmonton, AB, Canada.ORCID http://orcid.org/0000-0002-3203-2897
Matthew S MacauleyDepartment of Chemistry, University of Alberta, Edmonton, AB, Canada. macauley@ualberta.ca.ORCID http://orcid.org/0000-0003-4579-1048
University of Alberta · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Immunomodulatory Siglecs are controlled by their glycoprotein and glycolipid ligands. Siglec-glycolipid interactions are often studied outside the context of a lipid bilayer, missing the complex behaviors of glycolipids in a membrane. Through optimizing a liposomal formulation to dissect Siglec-glycolipid interactions, it is shown that Siglec-6 can recognize glycolipids independent of its canonical binding pocket, suggesting that Siglec-6 possesses a secondary binding pocket tailored for recognizing glycolipids in a bilayer. A panel of synthetic neoglycolipids is used to probe the specificity of this glycolipid binding pocket on Siglec-6, leading to the development of a neoglycolipid with higher avidity for Siglec-6 compared to natural glycolipids. This neoglycolipid facilitates the delivery of liposomes to Siglec-6 on human mast cells, memory B-cells and placental syncytiotrophoblasts. A physiological relevance for glycolipid recognition by Siglec-6 is revealed for the binding and internalization of extracellular vesicles. These results demonstrate a unique and physiologically relevant ability of Siglec-6 to recognize glycolipids in a membrane.

Indexed as

Extracellular VesiclesSialic Acid Binding Immunoglobulin-like LectinsFemaleGlycolipidsHumansLiposomesMast CellsMemory B CellsPlacentaPregnancyGlycolipidsLiposomesSialic Acid Binding Immunoglobulin-like Lectins

Identifiers

PMID37087495
PMCPMC10122656
OpenAlexW4366768510

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.