Characterization and functional analysis of serine proteinase and serine proteinase homologue from the swimming crab Portunus trituberculatus
文献类型：期刊论文
| 作者 | Song, Chengwen1,2 ; Cui, Zhaoxia1; Liu, Yuan1; Li, Qianqian1,2; Li, Xihong1,2; Shi, Guohui1,2; Wang, Chunlin3
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| 刊名 | FISH & SHELLFISH IMMUNOLOGY
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| 出版日期 | 2013-08-01 |
| 卷号 | 35期号:2页码:231-239 |
| 关键词 | Portunus trituberculatus Serine proteinase Proteolytic activity Bacterial-binding Antimicrobial activity |
| ISSN号 | 1050-4648 |
| 通讯作者 | Cui, ZX |
| 中文摘要 | Serine proteases (SPs), with their homologues (SPHs), a family of multifunctional proteins, play a crucial role in innate immune system. In our present study, we made an appropriate correction: serine protease homologue PtcSPH (Li et al., [1]) obtained from the swimming crab Portunus trituberculatus was actually a serine protease and re-designated as PtcSP. Sequence analysis revealed PtcSP and PtSP (Li et al., [2]) might be encoded by the same genomic locus and generated by alternative splicing of the pre-mRNA. Eight exons were identified in genomic DNA sequence of PtcSP. A comprehensive phylogenetic analysis was made combined with our previous reports (Cui et al., [3]; Li et al., [1,2]). The result showed SPs and SPHs of P. trituberculatus had different origins in gene evolution. To further characterize the function(s) of proteins, the recombinant serine proteases or homologues were assayed for various biological functions: proteinase activity, antimicrobial activity and microorganisms binding activity. The recombinant protein PtcSP exhibited trypsin-like protease activity and antibacterial activity. PtSPH1 (Li et al., [2]) lacked proteolytic activity but displayed binding activity to yeast and the crab pathogenic bacterium, Vibrio alginolyticus. Further, the N-terminal clip domain of PtcSP had antibacterial activity and the C-terminal SP-like domain had trypsin-like protease activity. (C) 2013 Elsevier Ltd. All rights reserved. |
| 英文摘要 | Serine proteases (SPs), with their homologues (SPHs), a family of multifunctional proteins, play a crucial role in innate immune system. In our present study, we made an appropriate correction: serine protease homologue PtcSPH (Li et al., [1]) obtained from the swimming crab Portunus trituberculatus was actually a serine protease and re-designated as PtcSP. Sequence analysis revealed PtcSP and PtSP (Li et al., [2]) might be encoded by the same genomic locus and generated by alternative splicing of the pre-mRNA. Eight exons were identified in genomic DNA sequence of PtcSP. A comprehensive phylogenetic analysis was made combined with our previous reports (Cui et al., [3]; Li et al., [1,2]). The result showed SPs and SPHs of P. trituberculatus had different origins in gene evolution. To further characterize the function(s) of proteins, the recombinant serine proteases or homologues were assayed for various biological functions: proteinase activity, antimicrobial activity and microorganisms binding activity. The recombinant protein PtcSP exhibited trypsin-like protease activity and antibacterial activity. PtSPH1 (Li et al., [2]) lacked proteolytic activity but displayed binding activity to yeast and the crab pathogenic bacterium, Vibrio alginolyticus. Further, the N-terminal clip domain of PtcSP had antibacterial activity and the C-terminal SP-like domain had trypsin-like protease activity. (C) 2013 Elsevier Ltd. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 学科主题 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 类目[WOS] | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 研究领域[WOS] | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 关键词[WOS] | PROPHENOLOXIDASE-ACTIVATING FACTOR ; CRAYFISH PACIFASTACUS-LENIUSCULUS ; FRESH-WATER CRAYFISH ; PROTEASE HOMOLOG ; RECOGNITION PROTEIN ; MOLECULAR-CLONING ; INNATE IMMUNITY ; HEMOCYTES ; MASQUERADE ; EXPRESSION |
| 收录类别 | SCI |
| 原文出处 | 10.1016/j.fsi.2013.04.024 |
| 语种 | 英语 |
| WOS记录号 | WOS:000322207500005 |
| 公开日期 | 2014-07-17 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/16537]  |
| 专题 | 海洋研究所_海洋生物技术研发中心 海洋研究所_实验海洋生物学重点实验室 海洋研究所_海洋生态与环境科学重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, EMBL, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China 3.Ningbo Univ, Sch Marine Sci, Ningbo 315211, Zhejiang, Peoples R China |
| 推荐引用方式 GB/T 7714 | Song, Chengwen,Cui, Zhaoxia,Liu, Yuan,et al. Characterization and functional analysis of serine proteinase and serine proteinase homologue from the swimming crab Portunus trituberculatus[J]. FISH & SHELLFISH IMMUNOLOGY,2013,35(2):231-239. |
| APA | Song, Chengwen.,Cui, Zhaoxia.,Liu, Yuan.,Li, Qianqian.,Li, Xihong.,...&Wang, Chunlin.(2013).Characterization and functional analysis of serine proteinase and serine proteinase homologue from the swimming crab Portunus trituberculatus.FISH & SHELLFISH IMMUNOLOGY,35(2),231-239. |
| MLA | Song, Chengwen,et al."Characterization and functional analysis of serine proteinase and serine proteinase homologue from the swimming crab Portunus trituberculatus".FISH & SHELLFISH IMMUNOLOGY 35.2(2013):231-239. |
入库方式： OAI收割
来源：海洋研究所
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