• Christine B Read, Joseph L Kuijper, Siv A Hjorth, Mark D Heipel, Xiaoting Tang, Andrew J Fleetwood, Jeffrey L Dantzler, Susanne N Grell, Jesper Kastrup, Camilla Wang, Cameron S Brandt, Anker J Hansen, Nicolai R Wagtmann, Wenfeng Xu, and Vibeke W Stennicke.
• Novo Nordisk A/S, DK-2760 Måløv, Denmark; and.
• J. Immunol. 2015 Feb 15;194(4):1417-21.

AbstractTriggering receptor expressed on myeloid cells (TREM)-1 is an orphan receptor implicated in innate immune activation. Inhibition of TREM-1 reduces sepsis in mouse models, suggesting a role for it in immune responses triggered by bacteria. However, the absence of an identified ligand has hampered a full understanding of TREM-1 function. We identified complexes between peptidoglycan recognition protein 1 (PGLYRP1) and bacterially derived peptidoglycan that constitute a potent ligand capable of binding TREM-1 and inducing known TREM-1 functions. Interestingly, multimerization of PGLYRP1 bypassed the need for peptidoglycan in TREM-1 activation, demonstrating that the PGLYRP1/TREM-1 axis can be activated in the absence of bacterial products. The role for PGLYRP1 as a TREM-1 activator provides a new mechanism by which bacteria can trigger myeloid cells, linking two known, but previously unrelated, pathways in innate immunity.Copyright © 2015 by The American Association of Immunologists, Inc.

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