Cited by 291Immune Response and InflammationInflammation biomarkers and pathwaysPhagocytosis and Immune Regulation

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Pattern Recognition by TREM-2: Binding of Anionic Ligands

Daws, Michael R, Sullam, Paul M, Niemi, Eréne C, Chen, Thomas T, Tchao, Nadia K, Seaman, William E·2003·The Journal of Immunology

DOI 10.4049/jimmunol.171.2.594

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Abstract

We recently described the cloning of murine triggering receptor expressed by myeloid cells (TREM) 2, a single Ig domain DNAX adaptor protein 12-associated receptor expressed by cells of the myeloid lineage. In this study, we describe the identification of ligands for TREM-2 on both bacteria and mammalian cells. First, by using a TREM-2A/IgG1-Fc fusion protein, we demonstrate specific binding to a number of Gram-negative and Gram-positive bacteria and to yeast. Furthermore, we show that fluorescently labeled Escherichia coli and Staphylococcus aureus bind specifically to TREM-2-transfected cells. The binding of TREM-2A/Ig fusion protein to E. coli can be inhibited by the bacterial products LPS, lipoteichoic acid, and peptidoglycan. Additionally, binding can be inhibited by a number of other anionic carbohydrate molecules, including dextran sulfate, suggesting that ligand recognition is based partly on charge. Using a sensitive reporter assay, we demonstrate activation of a TREM-2A/CD3ζ chimeric receptor by both bacteria and dextran sulfate. Finally, we demonstrate binding of TREM-2A/Ig fusion to a series of human astrocytoma lines but not to a variety of other cell lines. The binding to astrocytomas, like binding to bacteria, is inhibited by anionic bacterial products, suggesting either a similar charge-based ligand recognition method or overlapping binding sites for recognition of self- and pathogen-expressed ligands.

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Authors: Daws, M. R., Sullam, P. M., Niemi, E. C., Chen, T. T., Tchao, N. K., & Seaman, W. E.
Affiliations: San Francisco VA Medical Center (US)
Department of Immunology, Veterans Affairs Medical Center and University of California , San Francisco
University of California, San Francisco (US)
ORCID: Daws, Michael R
Sullam, Paul M
Chen, Thomas T
Venue: The Journal of Immunology
Publisher: Oxford University Press (OUP)
Published: 2003-07
Volume: 171
Issue: 2
Pages: 594-599
ISSN: 0022-1767 (ISSN-L)
1550-6606
DOI: 10.4049/jimmunol.171.2.594
OpenAlex: W2101372125
Cited by: 291
References: 44
Citations by year: 2026: 12 · 2025: 17 · 2024: 14 · 2023: 17 · 2022: 20 · 2021: 17 · 2020: 20 · 2019: 11 · 2018: 21 · 2017: 16 · 2016: 11 · 2015: 15 · 2014: 12 · 2013: 9 · 2012: 7
FWCI: 3.25
Type: journal article
Language: en
Open access: closed
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: The Journal of Immunology (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Veterans Affairs
National Cancer Institute (R01CA087922, R01 CA87922-01A1)
National Institute of Allergy and Infectious Diseases (AI41513, R01AI041513)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Immunology and Microbiology › Immunology › Inflammation biomarkers and pathways
Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
Keywords: TREM2, pattern recognition, myeloid cells, Gram-negative bacteria, Gram-positive bacteria, Escherichia coli, Staphylococcus aureus, yeast, lipopolysaccharide, lipoteichoic acid, peptidoglycan, dextran sulfate, astrocytoma, innate immunity, receptor activation
MeSH terms: Animals, Anions, Astrocytoma, Bacterial Adhesion, Binding, Competitive, Gram-Negative Bacteria, Gram-Positive Bacteria, Humans, Immunoglobulin Fc Fragments, Leukemia P388, Ligands, Lipopolysaccharides, Peptidoglycan, Protein Binding, Receptors, Immunologic, Recombinant Fusion Proteins, Solubility, Teichoic Acids, Transfection, Tumor Cells, Cultured, Dextran Sulfate, Jurkat Cells, Mice

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Pattern Recognition by TREM-2: Binding of Anionic Ligands

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