Analysis Of Network Of Proteins Interacting With Pattern Recognition Receptor PGLYRP2

Peptidoglycan recognition protein 2(PGLYRP2)is a pattern recognition receptor specifically expressed in liver tissues,which has been proven to be an anti-tumor marker associated with hepatocellular carcinoma and can reshape the tumor microenvironment by recruiting tumor infiltrating lymphocytes and induce chemokines to improve the antitumor immune response.On the basis of our previous studies,the study obtained PGLYRP2 interaction network through protein spectrum technology.We performed GO enrichment and KEGG pathway analysis of the interaction network and further verified the interaction proteins by Co-Immunoprecipitation(CO-IP)and screened a series of members of the RNA helicase family with DEAD-box conserved mode,pre-m RNA splicing factor rich in arginine/serine and RNA exosome complex members interacting with PGLYRP2.ATP-dependent DEAD-box family members,which constitute the largest RNA helicase family in human cells,can play the function of helicase.DDX3 X has been studied widely in the DEAD-box family,which can participate in the regulation of the early embryonic development,stress response,the occurrence and development of cancer and other biological events.These results show that PGLYRP2 interacts with DDX3 X in the domain of RNA helicase,suggesting that PGLYRP2 may regulate helicase function of DDX3 X.In addition,we used protein prediction tools to predict intrinsically disordered regions(IDRs)of PGLYRP2 and DDX3 X respectively,and found that both PGLYRP2 and DDX3 X have IDR regions.DDX3 X is involved in the regulation of series of biological processes,due to the dynamic signal networks that is established by the IDR-mediated phase separation.Therefore,we hypothesized that PGLYRP2 protein may regulate the immune response through IDR of DDX3X-mediated phase separation.