Research
| Title： | Functional characterization of a short peptidoglycan recognition protein from Chinese giant salamander (Andrias davidianus) |
|---|---|
| First author： | Qi, Zhitao; Ren, Shisi; Zhang, Qihuan; Zou, Jun; Xu, Qiaoqing; Wang, Zisheng; Qiao, Guo; Nie, Pin; Chang, Mingxian |
| Journal： | ONCOTARGET |
| Years： | 2017 |
| DOI： | 10.18632/oncotarget.21470 |
| Abstract： | Peptidoglycan (PGN) recognition proteins (PGRPs) are important pattern recognition receptors (PRRs) involved in immune defense against bacterial infections. In this study, a short PGRP (termed AdPGRP-S1) was cloned and functionally characterized from Chinese giant salamander (Andrias davidianus), the largest extant urodela amphibian species. AdPGRP-S1 was 184 aa in length and shared 38.7%-54.9% sequence identities with other vertebrates' short PGRPs. It contained one typical PGRP domain at the C-terminal region and several conserved amino acid (aa) residues involved in amidase and PGN binding. AdPGRP-S1 was constitutively expressed in all tissues examined, with the highest expression level seen in spleen and intestine. It has been shown that AdPGRP-S1 could bind and degrade Lys-PGN and Dap-PGN. Further, AdPGRP-S1 had antibacterial activity against the Gram-negative bacteria, Edwardsiella tarda, and was able to trigger the activation of NF-kappa B signaling. These results demonstrated that AdPGRP-S1 possesses multiple functions in pathogen recognition, mediating ceullular signaling, and initiating antibacterial response. This is the first functional study of a salamander PGRP, providing insight to further understand the functional evolution of verterbates' PGRPs. |
