Molecular cloning and functional characterization of a short peptidoglycan recognition protein (HcPGRPS1) from the freshwater mussel, Hyriopsis cumingi | |
Yang, Ziyan1,2; Li, Junhua3; Li, Ying1; Wu, Hongjuan1; Wang, Xiaoyan4 | |
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. |
个性服务 |
查看访问统计 |
相关权益政策 |
暂无数据 |
收藏/分享 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论