Cutting Edge: Identification of Neutrophil PGLYRP1 as a Ligand for TREM-1
Author(s) -
Christine B. Read,
Joseph L. Kuijper,
Siv A. Hjorth,
Mark Heipel,
Xiaoting Tang,
Andrew J. Fleetwood,
Jeffrey L. Dantzler,
S. Grell,
Jesper Kastrup,
Camilla Wang,
Cameron S. Brandt,
Anker Jón Hansen,
Nicolai Wagtmann,
Wenfeng Xu,
Vibeke W. Stennicke
Publication year - 2015
Publication title -
the journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.737
H-Index - 372
eISSN - 1550-6606
pISSN - 0022-1767
DOI - 10.4049/jimmunol.1402303
Subject(s) - peptidoglycan , innate immune system , microbiology and biotechnology , receptor , ligand (biochemistry) , immune system , biology , function (biology) , activator (genetics) , myeloid , bacteria , chemistry , immunology , biochemistry , genetics
Triggering 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.
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