Molecular cloning and functional characterization of a short peptidoglycan recognition protein (HcPGRPS1) from the freshwater mussel, Hyriopsis cumingi

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	Molecular cloning and functional characterization of a short peptidoglycan recognition protein (HcPGRPS1) from the freshwater mussel, Hyriopsis cumingi
	Yang, Ziyan 1,2; Li, Junhua 3; Li, Ying 1; Wu, Hongjuan 1; Wang, Xiaoyan 4
刊名	MOLECULAR IMMUNOLOGY
	2013-12-01
卷号	56 期号:4 页码:729-738
关键词	Hyriopsis cumingi Peptidoglycan recognition protein Innate immunity Peptidoglycan-binding activity Amidase activity Antibacterial activity
ISSN号	0161-5890
通讯作者	Wu, HJ (reprint author), Huazhong Univ Sci & Technol, Sch Environm Sci & Engn, Wuhan 430074, Hubei Province, Peoples R China.
中文摘要	Peptidoglycan recognition proteins (PGRPs), which are evolutionarily conserved from invertebrates to vertebrates, function as pattern-recognition and effector molecules in innate immunity. In the present study, a short-form PGRP, designated as HcPGRPS1 was identified from freshwater mussel Hyriopsis cumingi. The deduced amino acid sequence of HcPGRPS1 is composed of 235 residues which contains a conserved PGRP domain at the C-terminus. Sequence analysis showed that HcPGRPS1 shared high identities with other known PGRPs. The mRNA of HcPGRPS1 is constitutively expressed in a wide range of all tested tissues, with highest expression level in hepatopancreas, and its expression in tissues (gonad, nephridium, gill and foot) was up-regulated significantly after LPS or PGN stimulation (P<0.05). The recombinant protein of HcPGRPS1 exhibited binding activity and peptidoglycan-lytic amidase activity toward Lys-PGN from Staphylococcus aureus and DAP-PGN from Bacillus subtills. Furthermore, recombinant HcPGRPS1 displayed strong antibacterial activity to both Gram-negative bacteria Escherichia coli, Aeromonas hydrophila, Aeromonas sobria and Gram-positive bacteria S. aureus in the presence of Zn2+. These results suggested that HcPGRPS1 plays a multifunctional role in the defense and protection mechanisms of mussel innate immunity against infections. (C) 2013 Elsevier Ltd. All rights reserved.
英文摘要	Peptidoglycan recognition proteins (PGRPs), which are evolutionarily conserved from invertebrates to vertebrates, function as pattern-recognition and effector molecules in innate immunity. In the present study, a short-form PGRP, designated as HcPGRPS1 was identified from freshwater mussel Hyriopsis cumingi. The deduced amino acid sequence of HcPGRPS1 is composed of 235 residues which contains a conserved PGRP domain at the C-terminus. Sequence analysis showed that HcPGRPS1 shared high identities with other known PGRPs. The mRNA of HcPGRPS1 is constitutively expressed in a wide range of all tested tissues, with highest expression level in hepatopancreas, and its expression in tissues (gonad, nephridium, gill and foot) was up-regulated significantly after LPS or PGN stimulation (P<0.05). The recombinant protein of HcPGRPS1 exhibited binding activity and peptidoglycan-lytic amidase activity toward Lys-PGN from Staphylococcus aureus and DAP-PGN from Bacillus subtills. Furthermore, recombinant HcPGRPS1 displayed strong antibacterial activity to both Gram-negative bacteria Escherichia coli, Aeromonas hydrophila, Aeromonas sobria and Gram-positive bacteria S. aureus in the presence of Zn2+. These results suggested that HcPGRPS1 plays a multifunctional role in the defense and protection mechanisms of mussel innate immunity against infections. (C) 2013 Elsevier Ltd. All rights reserved.
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
类目[WOS]	Biochemistry & Molecular Biology ; Immunology
研究领域[WOS]	Biochemistry & Molecular Biology ; Immunology
关键词[WOS]	MESSENGER-RNA EXPRESSION ; GRAM-POSITIVE BACTERIA ; INNATE IMMUNITY ; ANTIBACTERIAL ACTIVITY ; ANOPHELES-GAMBIAE ; CRASSOSTREA-GIGAS ; CHLAMYS-FARRERI ; BOMBYX-MORI ; PGRP GENES ; DROSOPHILA
收录类别	SCI
资助信息	National Natural Science Foundation of China [31072209]
语种	英语
WOS记录号	WOS:000326203300048
公开日期	2014-01-24
内容类型	期刊论文
源URL	[http://ir.ihb.ac.cn/handle/342005/19779]
专题	水生生物研究所_鱼类生物学及渔业生物技术研究中心_期刊论文
作者单位	1.Huazhong Univ Sci & Technol, Sch Environm Sci & Engn, Wuhan 430074, Hubei Province, Peoples R China 2.North China Univ Water Resources & Elect Power, Sch Environm & Municipal Engn, Zhengzhou 450011, Henan Province, Peoples R China 3.Chinese Acad Sci, Grad Univ, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei Province, Peoples R China 4.Water Resources Off Hubei Prov, Wuhan 430071, Hubei Province, Peoples R China
推荐引用方式 GB/T 7714	Yang, Ziyan,Li, Junhua,Li, Ying,et al. Molecular cloning and functional characterization of a short peptidoglycan recognition protein (HcPGRPS1) from the freshwater mussel, Hyriopsis cumingi[J]. MOLECULAR IMMUNOLOGY,2013,56(4):729-738.
APA	Yang, Ziyan,Li, Junhua,Li, Ying,Wu, Hongjuan,&Wang, Xiaoyan.(2013).Molecular cloning and functional characterization of a short peptidoglycan recognition protein (HcPGRPS1) from the freshwater mussel, Hyriopsis cumingi.MOLECULAR IMMUNOLOGY,56(4),729-738.
MLA	Yang, Ziyan,et al."Molecular cloning and functional characterization of a short peptidoglycan recognition protein (HcPGRPS1) from the freshwater mussel, Hyriopsis cumingi".MOLECULAR IMMUNOLOGY 56.4(2013):729-738.