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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Laman AG,Lathe R,Savinov GV,Shepelyakovskaya AO,Boziev KhM,Baidakova LK,Chulin AN,Brovko FA,Svirshchevskaya EV,Kotelevtsev Y,Eliseeva IA,Guryanov SG,Lyabin DN,Ovchinnikov LP,Ivanov VTdoi
10.1016/j.febslet.2015.05.028subject
Has Abstractpub_date
2015-07-08 00:00:00pages
1819-24issue
15eissn
0014-5793issn
1873-3468pii
S0014-5793(15)00422-6journal_volume
589pub_type
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