Molecular and functional characterization of a short-type peptidoglycan recognition protein, PGRP-S in the amphibian Xenopus laevis

Jing Hou; Zhen Gan; Shan Nan Chen; Pin Nie

doi:10.1016/j.dci.2019.04.003

Molecular and functional characterization of a short-type peptidoglycan recognition protein, PGRP-S in the amphibian Xenopus laevis

Dev Comp Immunol. 2019 Sep:98:13-19. doi: 10.1016/j.dci.2019.04.003. Epub 2019 Apr 10.

Authors

Jing Hou¹, Zhen Gan¹, Shan Nan Chen², Pin Nie³

Affiliations

¹ State Key Laboratory of Freshwater Ecology and Biotechnology, Key Laboratory of Aquaculture Disease Control, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, Hubei Province, 430072, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
² State Key Laboratory of Freshwater Ecology and Biotechnology, Key Laboratory of Aquaculture Disease Control, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, Hubei Province, 430072, China.
³ State Key Laboratory of Freshwater Ecology and Biotechnology, Key Laboratory of Aquaculture Disease Control, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, Hubei Province, 430072, China; Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, Shandong Province, 266237, China; School of Marine Science and Engineering, Qingdao Agricultural University, Qingdao, Shandong Province, 266109, China. Electronic address: pinnie@ihb.ac.cn.

PMID: 30980872
DOI: 10.1016/j.dci.2019.04.003

Abstract

Peptidoglycan recognition proteins (PGRPs) are a family of pattern recognition receptors (PRRs) involved in host antibacterial responses, and their functions have been characterized in most invertebrate and vertebrate animals. However, little information is available regarding the function of frog PGRPs. In this study, a short-type PGRP (termed Xl-PGRP-S) gene was identified in the African clawed frog, Xenopus laevis. The predicted protein of Xl-PGRP-S contains several structural features known in PGRPs, including a typical PGRP domain and two closely spaced conserved cysteines. Xl-PGRP-S gene was constitutively expressed in all tissues examined, with the highest expression level observed in muscle. As a typical PRR, Xl-PGRP-S is inducible after peptidoglycan (PGN) stimulation, and has an ability to bind PGN. In addition, Xl-PGRP-S has been proven to have Zn²⁺-dependent amidase activity and antibacterial activity against Edwardsiella tarda. The present study represents the first discovery on the function of frog PGRPs, thus contributing to a better understanding of the functional evolution of PGRPs in early tetrapods.

Keywords: Amidase activity; Antibacterial activity; PGN; Short-type PGRP; Xenopus laevis.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amidohydrolases / genetics
Amidohydrolases / metabolism
Amino Acid Sequence
Animals
Anti-Bacterial Agents / metabolism
Anti-Bacterial Agents / pharmacology
Carrier Proteins / genetics*
Carrier Proteins / metabolism
Carrier Proteins / pharmacology
Cloning, Molecular
DNA, Complementary / chemistry
DNA, Complementary / genetics
Edwardsiella tarda / drug effects
Gene Expression Profiling / methods
Peptidoglycan / metabolism
Phylogeny
Protein Binding
Protein Isoforms / classification
Protein Isoforms / genetics
Protein Isoforms / metabolism
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Xenopus Proteins / genetics*
Xenopus Proteins / metabolism
Xenopus Proteins / pharmacology
Xenopus laevis / genetics*
Xenopus laevis / metabolism
Zinc / metabolism

Substances

Anti-Bacterial Agents
Carrier Proteins
DNA, Complementary
Peptidoglycan
Protein Isoforms
Xenopus Proteins
peptidoglycan recognition protein
Amidohydrolases
amidase
Zinc