Functional characterization of a short peptidoglycan recognition protein from Chinese giant salamander (Andrias davidianus)

Zhitao Qi; Shisi Ren; Qihuan Zhang; Jun Zou; Qiaoqing Xu; Zisheng Wang; Guo Qiao; Pin Nie; Mingxian Chang

doi:10.18632/oncotarget.21470

Functional characterization of a short peptidoglycan recognition protein from Chinese giant salamander (Andrias davidianus)

Zhitao Qi^*, Shisi Ren, Qihuan Zhang, Jun Zou, Qiaoqing Xu, Zisheng Wang, Guo Qiao, Pin Nie, Mingxian Chang

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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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-κB 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.

Original language	English
Pages (from-to)	99323-99335
Number of pages	13
Journal	Oncotarget
Volume	8
Issue number	59
DOIs	https://doi.org/10.18632/oncotarget.21470
Publication status	Published - 3 Oct 2017

Bibliographical note

This work was supported by the National Natural Science Foundation of China (Grant no. 31302221, 31172408 and 31272666) and Jiangsu Province (Grant no. BK20171274 and BK2011418), and partially by the Opening Project of Jiangsu Key Laboratory of Biochemistry and Biotechnology of Marine Wetland (Grant no. K2016-08). QZ was supported by the “Qinglan” project of Jiangsu province of China.

Keywords

Andrias davidianus
Functional analysis
Gene clone
Immune response
Immunity
Immunology and Microbiology Section
Peptidoglycan recognition protein

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Functional characterization of a short peptidoglycan recognition protein from Chinese giant salamander (Andrias davidianus)
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Cite this

@article{7f282629b5f843b5a880610070beabcb,

title = "Functional characterization of a short peptidoglycan recognition protein from Chinese giant salamander (Andrias davidianus)",

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-κB 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.",

keywords = "Andrias davidianus, Functional analysis, Gene clone, Immune response, Immunity, Immunology and Microbiology Section, Peptidoglycan recognition protein",

author = "Zhitao Qi and Shisi Ren and Qihuan Zhang and Jun Zou and Qiaoqing Xu and Zisheng Wang and Guo Qiao and Pin Nie and Mingxian Chang",

note = "This work was supported by the National Natural Science Foundation of China (Grant no. 31302221, 31172408 and 31272666) and Jiangsu Province (Grant no. BK20171274 and BK2011418), and partially by the Opening Project of Jiangsu Key Laboratory of Biochemistry and Biotechnology of Marine Wetland (Grant no. K2016-08). QZ was supported by the “Qinglan” project of Jiangsu province of China.",

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AU - Zou, Jun

AU - Xu, Qiaoqing

AU - Wang, Zisheng

AU - Qiao, Guo

AU - Nie, Pin

AU - Chang, Mingxian

N1 - This work was supported by the National Natural Science Foundation of China (Grant no. 31302221, 31172408 and 31272666) and Jiangsu Province (Grant no. BK20171274 and BK2011418), and partially by the Opening Project of Jiangsu Key Laboratory of Biochemistry and Biotechnology of Marine Wetland (Grant no. K2016-08). QZ was supported by the “Qinglan” project of Jiangsu province of China.

PY - 2017/10/3

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N2 - 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-κB 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.

AB - 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-κB 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.

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DO - 10.18632/oncotarget.21470

M3 - Article

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SP - 99323

EP - 99335

JO - Oncotarget

JF - Oncotarget

IS - 59

ER -

Functional characterization of a short peptidoglycan recognition protein from Chinese giant salamander (Andrias davidianus)

Abstract

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Keywords

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