Evidence map›Paper›PMID 41223255›Full record

ArticleScience advances2025

An ultrasensitive and modular platform to detect Siglec ligands and control immune cell function.

Zeinab Jame-Chenarboo, Edward N Schmidt, Madeline Crichton, Kei Takahashi-Yamashiro, Guilherme M Lima, Liany Luna-Dulcey, Jaesoo Jung, Sabine Ivison, Chris D St Laurent, Jhon R Enterina and 11 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

21 authors.

Zeinab Jame-ChenarbooDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0009-0003-4687-8652
Edward N SchmidtDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.
Madeline CrichtonDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0009-0003-8783-7881
Kei Takahashi-YamashiroDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0000-0002-7925-6636
Guilherme M LimaDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0000-0002-3268-6081
Liany Luna-DulceyDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.
Jaesoo JungDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0000-0002-9247-1066
Sabine IvisonDepartment of Surgery and BC Children's Hospital Research Institute, University of British Columbia, Vancouver, BC, Canada.
Chris D St LaurentDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0009-0007-9500-7406
Jhon R EnterinaDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada.ORCID 0000-0002-9137-3667
Sung-Yao LinDepartment of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada.ORCID 0009-0005-9252-0568
Susmita SarkarDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.
Maju JoeDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0000-0003-0664-5275
Fahima MozanehDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.
Reni JohnDepartment of Pathobiology, College of Veterinary Medicine, University of Illinois Urbana-Champaign, Urbana, IL, USA.
Som G NanjappaDepartment of Pathobiology, College of Veterinary Medicine, University of Illinois Urbana-Champaign, Urbana, IL, USA.ORCID 0000-0001-8022-1353
Stacy A MalakerDepartment of Chemistry, Yale University, New Haven, CT, USA.ORCID 0000-0003-2382-5067
Megan K LevingsDepartment of Surgery and BC Children's Hospital Research Institute, University of British Columbia, Vancouver, BC, Canada.ORCID 0000-0002-0305-5790
Jamey D MarthSanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA.
Ratmir DerdaDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0000-0003-1365-6570
Matthew S MacauleyDepartment of Chemistry, University of Alberta, Edmonton, Alberta, Canada.ORCID 0000-0003-4579-1048

Funding

Protein Glycosylation in the Coagulopathy and Inflammation of SepsisP01HL131474 · NHLBI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MAHAN, MICHAEL J · 2016 to 2025
$26.2M
GLYCOSYLTRANSFERASE FUNCTION IN DEVELOPMENT AND DISEASER01DK048247 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JAMEY MARTH · 1994 to 2026
$9.4M
Protein Sialylation and De-Sialyation in Cell Surface Glycoprotein Homeostasis and DiseaseR01AI151371 · NIAID · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARTH, JAMEY · 2021 to 2025
$2.4M
Immunity against fungal infectionsR01AI153522 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI NANJAPPA, SOMASHEKARAPPA GOWDA · 2021 to 2025
$2.3M
Regulation of Blood Glycoproteins by Lectin Receptors in Health and DiseaseR01HL158677 · NHLBI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI JAMEY MARTH · 2023 to 2026
$1.9M
NHLBI NIH HHS P01 HL131474NHLBI NIH HHS R01 HL158677NIAID NIH HHS R01 AI151371NIAID NIH HHS R01 AI153522NIDDK NIH HHS R01 DK048247
6 · The paper itself

Abstract

Siglecs are immunomodulatory receptors that regulate immune cell function. A fundamental challenge in studying Siglec-ligand interactions is the low affinity of Siglecs for their ligands. Inspired by how nature uses multivalency, we developed Siglec-liposomes as a highly multivalent and versatile platform for detecting Siglec glycan ligands in which recombinant Siglecs were conjugated to liposomes using the SpyCatcher-SpyTag system. Siglec-liposomes offer tunable multivalency and a modular assembly, enabling presentation of different Siglecs on the same liposome. Using Siglec-liposomes, we profiled Siglec ligands on human leukocytes, revealing distinct patterns of Siglec ligands. Moreover, Siglec-liposomes are in vivo compatible, where we demonstrated that Siglec-7-liposomes bind to the brain vasculature in a mucin domain-dependent manner. Given the abundance of Siglec ligands on T cells, we investigated whether Siglec-liposomes modulate T cell function and find that Siglec-7-liposomes increase T cell proliferation in an ST3Gal1-dependent and CD43-independent manner. Together, Siglec-liposomes are a versatile and sensitive tool for detecting Siglec ligands and immunomodulation.

Indexed as

LiposomesSialic Acid Binding Immunoglobulin-like LectinsT-LymphocytesAnimalsAntigens, Differentiation, MyelomonocyticCell ProliferationCHO CellsCricetinaeHumansLectinsLigandsMiceMice, Inbred C57BLAntigens, Differentiation, MyelomonocyticLectinsLigandsLiposomesSialic Acid Binding Immunoglobulin-like LectinsSIGLEC7 protein, human

Identifiers

PMID41223255
PMCPMC12609110

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Registered trials

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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.