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题名: Functional characterization of a short peptidoglycan recognition protein, PGRP5 in grass carp Ctenopharyngodon idella
作者: Li, Jun Hua1, 2; Chang, Ming Xian1; Xue, Na Na1, 2; Nie, P.1
通讯作者: Chang, MX (reprint author), Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Hubei Province, Peoples R China.
关键词: Peptidoglycan recognition protein ; PGRP5 ; Peptidoglycan-binding activity ; Amidase activity ; Grass carp
刊名: FISH & SHELLFISH IMMUNOLOGY
发表日期: 2013-08-01
DOI: 10.1016/j.fsi.2013.04.025
卷: 35, 期:2, 页:221-230
收录类别: SCI
文章类型: Article
部门归属: [Li, Jun Hua ; Chang, Ming Xian ; Xue, Na Na ; Nie, P.] Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei Province, Peoples R China ; [Li, Jun Hua ; Xue, Na Na] Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China
WOS标题词: Science & Technology ; Life Sciences & Biomedicine
资助者: National Natural Science Foundation of China [31172408]; National Basic Research Programme (973 Programme) of China [2009CB118703]
类目[WOS]: Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
研究领域[WOS]: Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
摘要: Peptidoglycan recognition proteins (PGRPs), which are evolutionarily conserved from insects to mammals, recognize bacterial peptidoglycan (PGN) and function in antibacterial innate immunity. In this study, a short-form PGRP, designated as gcPGRP5 was identified from grass carp Ctenopharyngodon idella. The deduced amino acid sequence of gcPGRP5 is composed of 180 residues with a conserved PGRP domain at the C-terminus. The gcPGRP5 gene consists of four exons and three introns, spacing approximately 2.3 kb in genomic sequence. Phylogenetic analysis demonstrated that the gcPGRP5 is clustered with other PGRP-S identified in teleost fish. The gcPGRP5 is constitutively expressed in all organs/tissues examined, and its expression was significantly induced in CIK cells treated with lipoteichoic acid (LTA), polyinosinic polycytidylic acid (Poly I:C) and PGN. Fluorescence analysis showed that gcPGRP5 is distributed in cytoplasm of CIK cells, and cell lysates from CIK cells transfected with pTurbo-gcPGRP5-GFP and ptGFP1-gcPGRP5 plasmids display the binding activity and peptidoglycan-lytic amidase activity toward Lys-PGN from Staphylococcus aureus and Dap-PGN from Bacillus subtilis. Furthermore, heat-shock protein70 (Hsp70), and MyD88, an adaptor molecule in Toll-like receptor pathway, had an increased expression in CIK cells overexpressed with gcPGRP5. It is thus indicated that gcPGRP5 exhibits amidase activity, and also possesses roles in anti-stress, and in Toll-like receptor signaling pathway. (C) 2013 Elsevier Ltd. All rights reserved.
英文摘要: Peptidoglycan recognition proteins (PGRPs), which are evolutionarily conserved from insects to mammals, recognize bacterial peptidoglycan (PGN) and function in antibacterial innate immunity. In this study, a short-form PGRP, designated as gcPGRP5 was identified from grass carp Ctenopharyngodon idella. The deduced amino acid sequence of gcPGRP5 is composed of 180 residues with a conserved PGRP domain at the C-terminus. The gcPGRP5 gene consists of four exons and three introns, spacing approximately 2.3 kb in genomic sequence. Phylogenetic analysis demonstrated that the gcPGRP5 is clustered with other PGRP-S identified in teleost fish. The gcPGRP5 is constitutively expressed in all organs/tissues examined, and its expression was significantly induced in CIK cells treated with lipoteichoic acid (LTA), polyinosinic polycytidylic acid (Poly I:C) and PGN. Fluorescence analysis showed that gcPGRP5 is distributed in cytoplasm of CIK cells, and cell lysates from CIK cells transfected with pTurbo-gcPGRP5-GFP and ptGFP1-gcPGRP5 plasmids display the binding activity and peptidoglycan-lytic amidase activity toward Lys-PGN from Staphylococcus aureus and Dap-PGN from Bacillus subtilis. Furthermore, heat-shock protein70 (Hsp70), and MyD88, an adaptor molecule in Toll-like receptor pathway, had an increased expression in CIK cells overexpressed with gcPGRP5. It is thus indicated that gcPGRP5 exhibits amidase activity, and also possesses roles in anti-stress, and in Toll-like receptor signaling pathway. (C) 2013 Elsevier Ltd. All rights reserved.
关键词[WOS]: L-ALANINE AMIDASE ; INNATE IMMUNITY ; POSITIVE BACTERIA ; ANTIBACTERIAL ACTIVITY ; MOLECULAR-CLONING ; DROSOPHILA ; EXPRESSION ; TOLL ; ZEBRAFISH ; RECEPTORS
语种: 英语
WOS记录号: WOS:000322207500004
ISSN号: 1050-4648
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.ihb.ac.cn/handle/342005/19581
Appears in Collections:鱼类生物学及渔业生物技术研究中心_期刊论文

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作者单位: 1.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei Province, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China

Recommended Citation:
Li, Jun Hua; Chang, Ming Xian; Xue, Na Na; Nie, P..Functional characterization of a short peptidoglycan recognition protein, PGRP5 in grass carp Ctenopharyngodon idella,FISH & SHELLFISH IMMUNOLOGY,2013,35(2):221-230
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