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 journalArticle

5 Citations (Scopus)
4 Downloads (Pure)

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 languageEnglish
Pages (from-to)99323-99335
Number of pages13
JournalOncotarget
Volume8
Issue number59
DOIs
Publication statusPublished - 3 Oct 2017

Fingerprint

Urodela
Peptidoglycan
amidase
Proteins
Edwardsiella tarda
Pattern Recognition Receptors
Amino Acids
Amphibians
Gram-Negative Bacteria
Bacterial Infections
Intestines
Vertebrates
Spleen
peptidoglycan recognition protein

Keywords

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

ASJC Scopus subject areas

  • Oncology

Cite this

Functional characterization of a short peptidoglycan recognition protein from Chinese giant salamander (Andrias davidianus). / Qi, Zhitao; Ren, Shisi; Zhang, Qihuan; Zou, Jun; Xu, Qiaoqing; Wang, Zisheng; Qiao, Guo; Nie, Pin; Chang, Mingxian.

In: Oncotarget, Vol. 8, No. 59, 03.10.2017, p. 99323-99335.

Research output: Contribution to journalArticle

Qi, Z, Ren, S, Zhang, Q, Zou, J, Xu, Q, Wang, Z, Qiao, G, Nie, P & Chang, M 2017, 'Functional characterization of a short peptidoglycan recognition protein from Chinese giant salamander (Andrias davidianus)', Oncotarget, vol. 8, no. 59, pp. 99323-99335. https://doi.org/10.18632/oncotarget.21470
Qi, Zhitao ; Ren, Shisi ; Zhang, Qihuan ; Zou, Jun ; Xu, Qiaoqing ; Wang, Zisheng ; Qiao, Guo ; Nie, Pin ; Chang, Mingxian. / Functional characterization of a short peptidoglycan recognition protein from Chinese giant salamander (Andrias davidianus). In: Oncotarget. 2017 ; Vol. 8, No. 59. pp. 99323-99335.
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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.",
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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.

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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.

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