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题名: Molecular cloning and functional characterization of a short peptidoglycan recognition protein (HcPGRPS1) from the freshwater mussel, Hyriopsis cumingi
作者: Yang, Ziyan1, 2; Li, Junhua3; Li, Ying1; Wu, Hongjuan1; Wang, Xiaoyan4
通讯作者: Wu, HJ (reprint author), Huazhong Univ Sci & Technol, Sch Environm Sci & Engn, Wuhan 430074, Hubei Province, Peoples R China.
关键词: Hyriopsis cumingi ; Peptidoglycan recognition protein ; Innate immunity ; Peptidoglycan-binding activity ; Amidase activity ; Antibacterial activity
刊名: MOLECULAR IMMUNOLOGY
发表日期: 2013-12-01
DOI: 10.1016/j.molimm.2013.06.019
卷: 56, 期:4, 页:729-738
收录类别: SCI
文章类型: Article
部门归属: [Yang, Ziyan ; Li, Ying ; Wu, Hongjuan] Huazhong Univ Sci & Technol, Sch Environm Sci & Engn, Wuhan 430074, Hubei Province, Peoples R China ; [Yang, Ziyan] North China Univ Water Resources & Elect Power, Sch Environm & Municipal Engn, Zhengzhou 450011, Henan Province, Peoples R China ; [Li, Junhua] Chinese Acad Sci, Grad Univ, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei Province, Peoples R China ; [Wang, Xiaoyan] Water Resources Off Hubei Prov, Wuhan 430071, Hubei Province, Peoples R China
WOS标题词: Science & Technology ; Life Sciences & Biomedicine
资助者: National Natural Science Foundation of China [31072209]
类目[WOS]: Biochemistry & Molecular Biology ; Immunology
研究领域[WOS]: Biochemistry & Molecular Biology ; Immunology
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.
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
语种: 英语
WOS记录号: WOS:000326203300048
ISSN号: 0161-5890
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.ihb.ac.cn/handle/342005/19779
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.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

Recommended Citation:
Yang, Ziyan; Li, Junhua; Li, Ying; Wu, Hongjuan; Wang, Xiaoyan.Molecular cloning and functional characterization of a short peptidoglycan recognition protein (HcPGRPS1) from the freshwater mussel, Hyriopsis cumingi,MOLECULAR IMMUNOLOGY,2013,56(4):729-738
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