The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Pattern Recognition by TREM-2: Binding of Anionic Ligands
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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“Sequence variants of the LPS-receptor TLR4 [84] and the LPS-binding receptor TREM2 [22] are also associated with an increased risk of AD, indicating additional genetic links between AD and endotoxin.”
From The endotoxin hypothesis of neurodegeneration (2019) · cites this paper as [22]
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“Three members of the mouse TREM family have been studied: TREM-1 (1, 4), TREM-2 (3, 5), and TREM-3 (2).”
BackgroundMethodInfluentialDirect Recognition of Cytomegalovirus by Activating and Inhibitory NK Cell Receptors
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Cited by
Sorted by citations
TREM2 Lipid Sensing Sustains the Microglial Response in an Alzheimer’s Disease Model
Wang, Y., Cella, M., Mallinson, K., Ulrich, J. D., Young, K. L., Robinette, M. L., Gilfillan, S., Krishnan, G. M., Sudhakar, S., Zinselmeyer, B. H., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.049 · Cited by 1,736
Systemic infections and inflammation affect chronic neurodegeneration
Perry, V. H., Cunningham, C., & Holmes, C. (2007) · Nature Reviews Immunology · doi:10.1038/nri2015 · Cited by 1,027
TREM2-mediated early microglial response limits diffusion and toxicity of amyloid plaques
Wang, Y., Ulland, T. K., Ulrich, J. D., Song, W., Tzaferis, J. A., Hole, J. T., Yuan, P., Mahan, T. E., Shi, Y., Gilfillan, S., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151948 · Cited by 840
CNS immune privilege: hiding in plain sight
Carson, M. J., Doose, J. M., Melchior, B., Schmid, C. D., & Ploix, C. C. (2006) · Immunological Reviews · doi:10.1111/j.1600-065x.2006.00441.x · Cited by 838
TREM2 — a key player in microglial biology and Alzheimer disease
Ulland, T. K., & Colonna, M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0072-1 · Cited by 735
Metadata
- 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)
- 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
- 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
- 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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