Abstract / Description of output
Abstract The bacterial cell wall muramyl dipeptides MDP and glucosaminyl-MDP (GMDP) are powerful immunostimulators but their binding target remains controversial. We previously reported expression cloning of GMDP-binding polypeptides and identification of Y-box protein 1 (YB-1) as their sole target. Here we show specific binding of GMDP to recombinant YB-1 protein and subcellular colocalization of YB-1 and GMDP. GMDP binding to YB-1 upregulated gene expression levels of NF-κB2, a mediator of innate immunity. Furthermore, YB-1 knockdown abolished GMDP-induced Nfkb2 expression. GMDP/YB-1 stimulation led to NF-κB2 cleavage, transport of activated NF-κB2 p52 to the nucleus, and upregulation of NF-κB2-dependent chemokine Cxcr4 gene expression. Therefore, our findings identify YB-1 as new target for muramyl peptide signaling.
Original language | English |
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Article number | 37184 |
Pages (from-to) | 1819-1824 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 589 |
Issue number | 15 |
DOIs | |
Publication status | Published - 3 Jul 2015 |
Keywords / Materials (for Non-textual outputs)
- Glucosaminyl-muramyl dipeptide
- Innate immunity
- Muramyl peptide
- Y-box protein 1