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Immune recognition, antimicrobial and opsonic activities mediated by a sialic acid binding lectin fr

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Immune recognition, antimicrobial and opsonic activities mediated by a sialic acid binding lectin from Ruditapes philippinarum
Li, SQ; Ruan, ZL; Yang, XY; Li, MZ; Yang, DL
发表期刊FISH & SHELLFISH IMMUNOLOGY
ISSN1050-4648
2019-10
卷号93页码:66-72
关键词Ruditapes philippinarumSialic acid-binding lectinPattern recognition receptorImmune recognition
研究领域Fisheries; Immunology; Marine & Freshwater Biology; Veterinary Sciences
DOI10.1016/j.fsi.2019.07.027
产权排序[Li, Shengqiang; Ruan, Zeli; Yang, Xiyun; Li, Mingzhu] Ludong Univ, Coll Agr, Yantai, Peoples R China; [Yang, Dinglong] Chinese Acad Sci, Yantai Inst Coastal Zone Res, Muping Coastal Environm Res Stn, Yantai 264003, Peoples R China; [Yang, Dinglong] Chinese Acad Sci, Ctr Ocean Megasci, Qingdao 266071, Shandong, Peoples R China
通讯作者Li, Mingzhu(ldulimingzhu@163.com); Yang, Dinglong(dlyang@yic.ac.cn)
作者部门中国科学院牟平海岸带环境综合试验站
英文摘要In the present study, a sialic acid-binding lectin was identified and characterized from Manila clam Ruditapes philippinarum (designed as RpSABL-1). Multiple alignments strongly suggested that RpSABL-1 was a new member of the sialic acid-binding lectin family. In non-stimulated clams, RpSABL-1 transcripts were constitutively expressed in all five tested tissues, especially in hepatopancreas. After Vibrio anguillarum challenge, the expression of RpSABL-1 mRNA was significantly up-regulated at 6 h (P < 0.05), 12 h (P < 0.01) and 24 h (P < 0.01). Recombinant RpSABL-1 protein (rRpSABL-1) displayed apparent binding activities towards lipopolysaccharides (LPS) and peptidoglycan (PGN), but not to glucan or chitin in vitro. Coinciding with the PAMPs binding assay, rRpSABL-1 exhibited obvious agglutination activities against Gram-positive bacterium Staphyloccocus aureus, Gram-negative bacteria Escherichia coli, V. anguillarum and Vibrio harveyi. Meanwhile, rRpSABL-1 showed antibacterial activities against E. coli, and biofilm formation of E. coli could also be inhibited after incubated with rRpSABL-1. Moreover, the encapsulation, phagocytosis and chemotactic ability of hemocytes could be enhanced by rRpSABL-1. All these results suggested that RpSABL-1 could function as a pattern recognition receptor with versatile functions in the innate immune responses of R. philippinarum.
文章类型Article
资助机构Strategic Priority Research Program of the Chinese Academy of SciencesChinese Academy of Sciences [XDA23050303]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China [41806196]; Key Research Program of the Chinese Academy of SciencesChinese Academy of Sciences [KFJ-STS-ZDTP-023]; Natural Science Foundation of Shandong ProvinceNatural Science Foundation of Shandong Province [ZR2019BD022]; Youth Innovation Promotion Association CAS [2016196]
收录类别SCI
语种英语
关键词[WOS]C-TYPE LECTIN; ANTIBACTERIAL ACTIVITY; C1Q-DOMAIN-CONTAINING PROTEIN; CHLAMYS-FARRERI; EXPRESSION; PEPTIDE; MECHANISM; MONOCYTES; DEFENSIN; DISEASE
研究领域[WOS]Fisheries; Immunology; Marine & Freshwater Biology; Veterinary Sciences
WOS记录号WOS:000488998300008
引用统计被引频次:3[WOS][WOS记录][WOS相关记录]
文献类型期刊论文
条目标识符http://ir.yic.ac.cnhttp://ir.yic.ac.cn/handle/133337/24845
专题支撑部门_中国科学院牟平海岸带环境综合试验站
海岸带生物学与生物资源利用重点实验室_海岸带生物资源高效利用研究与发展中心

作者单位1.Ludong Univ, Coll Agr, Yantai, Peoples R China;
2.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Muping Coastal Environm Res Stn, Yantai 264003, Peoples R China;
3.Chinese Acad Sci, Ctr Ocean Megasci, Qingdao 266071, Shandong, Peoples R China

推荐引用方式
GB/T 7714Li, SQ,Ruan, ZL,Yang, XY,et al. Immune recognition, antimicrobial and opsonic activities mediated by a sialic acid binding lectin from Ruditapes philippinarum[J]. FISH & SHELLFISH IMMUNOLOGY,2019,93:66-72.
APALi, SQ,Ruan, ZL,Yang, XY,Li, MZ,&Yang, DL.(2019).Immune recognition, antimicrobial and opsonic activities mediated by a sialic acid binding lectin from Ruditapes philippinarum.FISH & SHELLFISH IMMUNOLOGY,93,66-72.
MLALi, SQ,et al."Immune recognition, antimicrobial and opsonic activities mediated by a sialic acid binding lectin from Ruditapes philippinarum".FISH & SHELLFISH IMMUNOLOGY 93(2019):66-72.


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