ArticleNature communications2023
Structural insights into Siglec-15 reveal glycosylation dependency for its interaction with T cells through integrin CD11b.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 51 citations in OpenAlex.
- α2,6-Sialoglycan-regulated antitumor immunity of tumor-infiltrating CD8Nature chemical biology · 2026Article
- Post-translational modifications of integrins: molecular mechanisms and pathological implications.Cellular and molecular life sciences : CMLS · 2026Review
- Siglec‑15 dysregulation and its therapeutic implications in new‑onset type 1 diabetes.International journal of molecular medicine · 2026Article
- PRAS40 activates the IRE1α-XBP-1-mediated unfolded protein response to exacerbate colorectal cancer by enhancing ST6Gal1-dependent α-2, 6 sialylation of GRP78.Neoplasia (New York, N.Y.) · 2026Article
- Sialic acids modulate immune responses in cancer: Therapeutic opportunities.The Journal of biological chemistry · 2026Review
- Innovative immunotherapy approaches: harnessing synergy of dual checkpoint blockade in oncology.Naunyn-Schmiedeberg's archives of pharmacology · 2026Review
- Writers and readers of sialylation in immunoregulation in cancer.The Journal of biological chemistry · 2026Review
- Transmembrane lectins in cancer immunity: emerging drivers of myeloid-mediated immunosuppression.Frontiers in immunology · 2026Review
- Tuning CAR-T cells by targeting cancer-associated glycan in pancreatic cancer.Nature communications · 2025Article
- Tumor-associated macrophages: untapped molecular targets to improve T cell-based immunotherapy.Molecular cancer · 2025Review
- Chimerolectins: Classification, structural architecture, and functional perspectives.Protein science : a publication of the Protein Society · 2025Review
- Tumor glyco-immunology, glyco-immune checkpoints and immunotherapy.Journal for immunotherapy of cancer · 2025Review
- NXPE1 alters the sialoglycome by acetylating sialic acids in the human colon.Nature communications · 2025Article
- Anti-Tumor Activities of Anti-Siglec-15 Chimeric Heavy-Chain Antibodies.International journal of molecular sciences · 2025Article
- Siglec-15 antibody-GM-CSF chimera suppresses tumor progression via reprogramming tumor-associated macrophages.Journal for immunotherapy of cancer · 2025Article
- Siglec-targeted liposomes to identify sialoglycans present on fungal pathogens.Antimicrobial agents and chemotherapy · 2025Article
- Metabolic Probing of Sialylated Glycoconjugates with Fluorine-Selenol Displacement Reaction (FSeDR).ACS bio & med chem Au · 2025Article
- Article
- Killing two birds with one stone: Siglec-15 targeting integrated bioactive glasses hydrogel for treatment of breast cancer bone metastasis.Materials today. Bio · 2024Article
- Enzyme-Sialylation-Controlled Chemical Sulfation of Glycan Epitopes for Decoding the Binding of Siglec Ligands.Journal of the American Chemical Society · 2024Article
Corrections and comments
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Authors and funding
22 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sialic acid-binding Ig-like lectin 15 (Siglec-15) is an immune modulator and emerging cancer immunotherapy target. However, limited understanding of its structure and mechanism of action restrains the development of drug candidates that unleash its full therapeutic potential. In this study, we elucidate the crystal structure of Siglec-15 and its binding epitope via co-crystallization with an anti-Siglec-15 blocking antibody. Using saturation transfer-difference nuclear magnetic resonance (STD-NMR) spectroscopy and molecular dynamics simulations, we reveal Siglec-15 binding mode to α(2,3)- and α(2,6)-linked sialic acids and the cancer-associated sialyl-Tn (STn) glycoform. We demonstrate that binding of Siglec-15 to T cells, which lack STn expression, depends on the presence of α(2,3)- and α(2,6)-linked sialoglycans. Furthermore, we identify the leukocyte integrin CD11b as a Siglec-15 binding partner on human T cells. Collectively, our findings provide an integrated understanding of the structural features of Siglec-15 and emphasize glycosylation as a crucial factor in controlling T cell responses.
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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.