The human TREM gene cluster at 6p21.1 encodes both activating and inhibitory single IgV domain receptors and includes NKp44

Allcock, Richard J. N.; Barrow, Alexander D.; Forbes, Simon; Beck, Stephan; Trowsdale, John

doi:10.1002/immu.200310033

Cited by 150 publications

(124 citation statements)

References 37 publications

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“…Constitutive expression of TREM-2 by cultured human ectocervical, endocervical, vaginal, ME-180, and HeLa cells was detected by flow cytometry (Figure 7). As a positive control, THP-1 cells were found to express TREM-2 as reported previously (40). Immunohistochemical staining also showed constitutive expression of TREM-2 by fallopian tubes as seen in the photomicrographs in Figure 8.…”

Section: Trem-2 Expression By Human Reproductive Tract Epithelial Cellssupporting

confidence: 83%

TREM-2 binds to lipooligosaccharides of Neisseria gonorrhoeae and is expressed on reproductive tract epithelial cells

et al. 2008

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Triggering receptor expressed on myeloid cells-2 (TREM-2) is an innate immune receptor that initiates cellular activation upon ligation. In this study, we examined the interaction of TREM-2 with Neisseria gonorrhoeae using murine TREM-2A as it has been reported to recognize bacterial ligands. Using a whole bacteria ELISA, TREM-2A bound to all 6 strains in variable degrees. Far western blots of gonococcal outer membranes revealed TREM-2A binding to lipooligosaccharide (LOS) and Opa protein with predominant binding to LOS. Binding of TREM-2A to LOS was confirmed by ELISA and surface plasmon resonance. O-deacylation of the lipid A significantly reduced binding. Flow cytometry and reporter cell assays showed that gonococci bound to TREM-2A-transfected cells and induced transmembrane signaling. In humans, TREM-2 was constitutively expressed by genitourinary and fallopian tube epithelial cells, both of which are primary targets of gonococcal invasion. Ligation of TREM-2 by LOS induced IL-6 production in HeLa cervical carcinoma cells. To our knowledge, this is the first report of the expression of human TREM-2 by cells deriving from a non-myeloid lineage. We conclude that gonococci can interact with TREM-2 receptors through binding to LOS and Opa protein and initiate cell signaling and cytokine production.

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Section: Trem-2 Expression By Human Reproductive Tract Epithelial Cellssupporting

confidence: 83%

TREM-2 binds to lipooligosaccharides of Neisseria gonorrhoeae and is expressed on reproductive tract epithelial cells

et al. 2008

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“…Also, it should be noted that in Nasu-Hakola disease patients, some of the reported mutations in TREM-2 might still permit the expression of a secreted form of TREM-2. Likewise, DAP12-deficient humans and mice may express secreted TREM-2 (18,19).…”

Section: Discussionmentioning

confidence: 99%

“…Thus, TREM-2 binding of its astrocyte ligand may allow adhesion of myeloid cells to astrocytes and thereby assist in localization of the myeloid cells or contribute to the stability of the cell-cell interaction. Also, TREM-2 may have activity as a soluble protein, independent of transmembrane signaling (18,19).…”

Section: Discussionmentioning

confidence: 99%

Pattern Recognition by TREM-2: Binding of Anionic Ligands

Daws

Sullam

Niemi³

et al. 2003

The Journal of Immunology

253

233

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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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“…Cell line RNAs were made as previously described (32). Tissue cDNA was a gift from Dr. D. Simmons (Celltech Group, Berkshire, U.K.).…”

Section: Rt-pcrmentioning

confidence: 99%

Two Human ULBP/RAET1 Molecules with Transmembrane Regions Are Ligands for NKG2D

Bacon

Eagle

Meyer

et al. 2004

The Journal of Immunology

Self Cite

156

150

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We characterized two novel members of the RAET1/ULBP gene cluster, RAET1E and RAET1G. The encoded proteins were similar to the ULBP in their class I-like α1 and α2 domains, but differed in that, instead of being GPI-anchored, their sequences were type 1 membrane-spanning molecules. Both proteins were capable of being expressed at the cell surface. Both proteins bound the activating receptor NKG2D, and RAET1G bound the human CMV protein UL16. The expression of diverse NKG2D-binding molecules in different tissues and with different properties is consistent with multiple modes of infection- or stress-induced activation.

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The human TREM gene cluster at 6p21.1 encodes both activating and inhibitory single IgV domain receptors and includes NKp44

Cited by 150 publications

References 37 publications

TREM-2 binds to lipooligosaccharides of Neisseria gonorrhoeae and is expressed on reproductive tract epithelial cells

TREM-2 binds to lipooligosaccharides of Neisseria gonorrhoeae and is expressed on reproductive tract epithelial cells

Pattern Recognition by TREM-2: Binding of Anionic Ligands

Two Human ULBP/RAET1 Molecules with Transmembrane Regions Are Ligands for NKG2D

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