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A lysin motif-containing protein (SpLysMD3) functions as a PRR involved in the antibacterial responses of mud crab, Scylla paramamosain

文献类型： 外文期刊

作者： Wang, Yue 1 ; Wang, Xue-Peng 3 ; Zhang, Bin 4 ; Li, Zhi-Min 2 ; Yang, Li-Guo 2 ; Li, Xin-Cang 2 ; Ma, Hongyu 1 ;

作者机构： 1.Shantou Univ, Inst Marine Sci, Guangdong Prov Key Lab Marine Biotechnol, Shantou 515063, Peoples R China

2.Chinese Acad Fishery Sci, East China Sea Fisheries Res Inst, Key Lab East China Sea Fishery Resources Exploita, Minist Agr, Shanghai 200090, Peoples R China

3.Shandong Agr Univ, Shandong Prov Key Lab Anim Biotechnol & Dis Contr, Tai An 271018, Shandong, Peoples R China

4.Yantai Nanshan Univ, Sch Business, Yantai 265706, Peoples R China

5.Shantou Univ, STU UMT Joint Shellfish Res Lab, Shantou 515063, Peoples R China

关键词： LysM protein; PRR; Binding activity; Bacterial clearance; AMPs; Scylla paramamosain

期刊名称：FISH & SHELLFISH IMMUNOLOGY （ 影响因子：4.581； 五年影响因子：4.851 ）

ISSN： 1050-4648

年卷期： 2020 年 97 卷

页码：

收录情况： SCI

摘要： Lysin motif (LysM)-containing proteins function as pattern-recognition receptors in plants to recognize different N-acetylglucosamine-containing ligands, thereby triggering specific defense responses against pathogens. However, the biological functions of these proteins in animals remain unclear. In this study, we characterized a novel LysM protein, designated as SpLysMD3, in mud crab Scylla paramamosain. The cDNA sequence of SpLysMD3 had 1058 bp with an open reading frame of 840 bp encoding a protein with 279 amino acid residues. The deduced protein contained a LysM domain and a transmembrane region. SpLysMD3 was highly expressed in gills, intestine, muscle, and hemocytes and upregulated after challenges with bacteria, suggesting that it may be involved in antibacterial defense. Binding assay showed that SpLysMD3 possessed specific binding activities to all tested microorganisms as well as bacterial cell wall components lipopolysaccharide (LPS) and peptidoglycan (PGN), indicating that SpLysMD3 was an important LPS- and PGN-binding protein in mud crab. Bacterial clearance assay revealed that coating bacteria with SpLysMD3 accelerated bacterial clearance in vivo. The promotion of bacterial clearance by SpLysMD3 was further determined by using SpLysMD3-silenced crabs injected with S. aureus or V. paraltemolyticus. Silencing SpLysMD3 dramatically suppressed the bacterial clearance. Meanwhile, knockdown of SpLysMD3 also severely impaired the expression of a specific set of antimicrobial peptides (AMPs); moreover, SpLysMD3 overexpression can enhance the promoter activity of SpALF2. These results suggested that SpLysMD3 affected bacterial clearance by regulating AMPs. Collectively, all the results demonstrated that SpLysMD3 may function as a potential receptor involved in innate immunity by binding to LPS and PGN and by regulating AMPs to eliminate invading pathogen. This study provided new insights into the biological functions of LysM proteins in animals and the mechanisms underlying the antibacterial activity of crustaceans.

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