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Characterization and functional analysis of a novel mannose-binding lectin from the swimming crab Portunus trituberculatus
Zhang, Mengjie1,3,4; Liu, Yuan1,2,3; Song, Chengwen1,2,3; Ning, Junhao1,3,4; Cui, Zhaoxia2,5
2019-06-01
Source PublicationFISH & SHELLFISH IMMUNOLOGY
ISSN1050-4648
Volume89Pages:448-457
Corresponding AuthorCui, Zhaoxia(cuizhaoxia@nbu.edu.cn)
AbstractMannose-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.
KeywordPortunus trituberculatus Mannose-binding lectin Pattern recognition receptor Antimicrobial activities
DOI10.1016/j.fsi.2019.04.007
Indexed BySCI
Language英语
Funding ProjectNational 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 Research AreaFisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS SubjectFisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS IDWOS:000469897700051
PublisherACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Citation statistics
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/161617
Collection实验海洋生物学重点实验室
Corresponding AuthorCui, Zhaoxia
Affiliation1.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
First Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Recommended Citation
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.
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