Characterization and functional analysis of a novel mannose-binding lectin from the swimming crab Portunus trituberculatus
文献类型：期刊论文
| 作者 | Zhang, Mengjie1,3,4 ; Liu, Yuan1,2,3; Song, Chengwen1,2,3; Ning, Junhao1,3,4; Cui, Zhaoxia2,5
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| 刊名 | FISH & SHELLFISH IMMUNOLOGY
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| 出版日期 | 2019-06-01 |
| 卷号 | 89页码:448-457 |
| 关键词 | Portunus trituberculatus Mannose-binding lectin Pattern recognition receptor Antimicrobial activities |
| ISSN号 | 1050-4648 |
| DOI | 10.1016/j.fsi.2019.04.007 |
| 通讯作者 | Cui, Zhaoxia(cuizhaoxia@nbu.edu.cn) |
| 英文摘要 | Mannose-binding lectin (MBL) is a pattern recognition receptor (PRR) that plays an important role in the innate immune response. In this study, a novel mannose-binding lectin was cloned from the swimmimg crab Portunus trituberculatus (designated as PtMBL). The complete cDNA of PtMBL gene was 1208 bp in length with an open reading frame (ORF) of 732 bp that encoded 244 amino acid proteins. PtMBL shared lower amino acid similarity with other MBLs, yet it contained the conserved carbohydrate-recognition domain (CRD) with QPD motif and was clearly member of the collectin family. PtMBL transcripts were mainly detected in eyestalk and gill with sexually dimorphic expression. The temporal expression of PtMBL in hemocytes showed different activation times after challenged with Vibrio alginolyticus, Micrococcus luteus and Pichia pastoris. The recombinant PtMBL protein revealed antimicrobial activity against the tested Gram-negative and Gram-positive bacteria. It could also bind and agglutinate (Ca2+-dependent) both bacteria and yeast. Furthermore, the agglutinating activity could be inhibited by both D-galactose and D-mannose, suggesting the broader pathogen-associated molecular patterns (PAMPs) recognition spectrum of PtMBL. These results together indicate that PtMBL could serve as not only a PRR in immune recognition but also a potential antibacterial protein in the innate immune response of crab. |
| 资助项目 | National Key R&D Program of China[2018YFD0900303] ; National Natural Science Foundations of China[41776159] ; Scientific and Technological Innovation Project of Qingdao National Laboratory for Marine Science and Technology[2015ASKJ02] ; Natural Science Foundation of Shandong Province[ZR2017QD001] |
| WOS研究方向 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 语种 | 英语 |
| WOS记录号 | WOS:000469897700051 |
| 出版者 | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/161616]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 通讯作者 | Cui, Zhaoxia |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, CAS Key Lab Expt Marine Biol, Qingdao 266071, Shandong, Peoples R China 2.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266071, Shandong, Peoples R China 3.Chinese Acad Sci, Ctr Ocean Mega Sci, Qingdao 266071, Shandong, Peoples R China 4.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 5.Ningbo Univ, Sch Marine Sci, Ningbo 315211, Zhejiang, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, Mengjie,Liu, Yuan,Song, Chengwen,et al. Characterization and functional analysis of a novel mannose-binding lectin from the swimming crab Portunus trituberculatus[J]. FISH & SHELLFISH IMMUNOLOGY,2019,89:448-457. |
| APA | Zhang, Mengjie,Liu, Yuan,Song, Chengwen,Ning, Junhao,&Cui, Zhaoxia.(2019).Characterization and functional analysis of a novel mannose-binding lectin from the swimming crab Portunus trituberculatus.FISH & SHELLFISH IMMUNOLOGY,89,448-457. |
| MLA | Zhang, Mengjie,et al."Characterization and functional analysis of a novel mannose-binding lectin from the swimming crab Portunus trituberculatus".FISH & SHELLFISH IMMUNOLOGY 89(2019):448-457. |
入库方式： OAI收割
来源：海洋研究所
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