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Pattern Recognition by TREM-2: Binding of Anionic Ligands
Michael R. Daws, Paul M. Sullam, Eréne C. Niemi, Thomas T. Chen, Nadia K. Tchao, William E. Seaman. The Journal of Immunology, 2003-07-01
Topic: Brain proteins, microglia and lab models
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/CD3zeta 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.
Why it matters
Lab experiments showed that TREM-2, a receptor on myeloid immune cells, binds specifically to a number of bacteria and yeast and to some human astrocytoma cell lines. Binding was blocked by anionic (negatively charged) molecules, suggesting TREM-2 recognizes its targets partly by charge.
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How this study scored 45/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it. We have no data on strength of evidence, so that was left out: it earned 43 of the 95 points we could judge it on, which is 45 out of 100.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (The Journal of Immunology) |
| Journal's citation record | 4 / 4 | The Journal of Immunology: journal h-index 531 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | — / 5 | No evidence rating recorded — left out of this score |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 2003 — older than 20 years, still counted |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 292 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 11.7 citations a year over 25 year(s) since 2003 |
| Impact for its field and year | 3 / 6 | Cited 3.1× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 0 / 6 | No other study in this library cites it |
| Still being cited | 2 / 4 | Cited 44 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author William E. Seaman: h-index 56 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | University of California, San Francisco: institution h-index 1,915 (OpenAlex) |
| Multi-centre collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 12847223) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Points | 43 / 95 | Scored on 19 of 20 parts. We have no data for the rest, so they are left out: 43 of the 95 points we could judge it on is 45 out of 100. |
| Total | 45 / 100 | — |
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Cite this study APA, Vancouver, BibTeX · download .bib or .ris
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. Check the citation against the original before you use it.
APA 7th
Daws, M. R., Sullam, P. M., Niemi, E. C., Chen, T. T., Tchao, N. K., & Seaman, W. E. (2003). Pattern Recognition by TREM-2: Binding of Anionic Ligands. The Journal of Immunology. https://doi.org/10.4049/jimmunol.171.2.594
Vancouver
Daws MR, Sullam PM, Niemi EC, Chen TT, Tchao NK, Seaman WE. Pattern Recognition by TREM-2: Binding of Anionic Ligands. The Journal of Immunology. 2003. doi:10.4049/jimmunol.171.2.594. PMID: 12847223.
BibTeX
@article{daws2003-12847223,
author = {Daws, Michael R. and Sullam, Paul M. and Niemi, Eréne C. and Chen, Thomas T. and Tchao, Nadia K. and Seaman, William E.},
title = {{Pattern Recognition by TREM-2: Binding of Anionic Ligands}},
journal = {The Journal of Immunology},
year = {2003},
doi = {10.4049/jimmunol.171.2.594},
pmid = {12847223},
url = {https://doi.org/10.4049/jimmunol.171.2.594}
}
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