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Two short peptidoglycan recognition proteins from Crassostrea gigas with similar structure exhibited different PAMP binding activity
Yang, Chuanyan1; Wang, Lingling1,2; Jia, Zhihao3; Yi, Qilin1; Xu, Qingsong1; Wang, Weilin3; Gong, Changhao1; Liu, Conghui3; Song, Linsheng1,2,4
2017-05-01
Source PublicationDEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume70Pages:9-18
SubtypeArticle
AbstractPeptidoglycan recognition protein (PGRP) is an essential molecule in innate immunity for both invertebrates and vertebrates, owing to its prominent ability in specifically recognizing bacterial peptidoglycan (PGN) and eliminating the invading bacteria. In the present study, the full length cDNA of two PGRP genes, CgPGRPS2 and CgPGRPS4, were cloned from oyster Crassostrea gigas. Their amino acid sequences both contained one signal peptide, one typical PGRP/amidase domain with conserved catalytic residues responsible for amidase activity (55H, 90Y, 164H, 172C in CgPGRPS2, and 98H, 133Y, 207H, 215C in CgPGRPS4), and specific PGN recognition (84R, 85W, 104R, 109V in CgPGRPS2, and 127G, 128W, 147R, 152V in CgPGRPS4), and they shared 55.9% sequente similarity. The mRNA transcripts of CgPGRPS2 and CgPGRPS4 were constitutively expressed in all the examined tissues, including haemocytes, hepatopancreas, mantle, gonad, heart, adductor muscle and gill, with the highest expression level in adductor muscle and hepatopancreas, respectively. Both CgPGRPS2 and CgPGRPS4 proteins were mainly localized in the cytoplasma. The recombinant protein of CgPGRPS2 (rCgPGRPS2) could bind lipopolysaccharide (LPS), PGN and mannan (Man), as well as various microorganisms including Gram-negative bacteria Escherichia coli, Vibrio anguillarum, Gram-positive bacteria Staphylococcus aureus and fungi Yarrowia lipolytica. The recombinant protein of CgPGRPS4 (rCgPGRPS4) exhibited higher binding affinity to PGN, lower binding affinity to LPS, while no binding activity to Man and Y. lipolytica. The results indicated that CgPGRPS2 and CgPGRPS4 could function as pattern recognition receptors (PRR) in the innate immune response of oyster, and they exhibited a certain degree of functional differentiation in recognition of Man. (C) 2016 Elsevier Ltd. All rights reserved.
KeywordCrassostrea Gigas Pgrp Innate Immunity Pattern Recognition Receptor Pamp Binding Activity
DOI10.1016/j.dci.2016.12.009
Indexed BySCI
Language英语
WOS IDWOS:000394635500002
Citation statistics
Cited Times:6[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.qdio.ac.cn/handle/337002/136799
Collection实验海洋生物学重点实验室
Affiliation1.Dalian Ocean Univ, Liaoning Key Lab Marine Anim Immunol & Dis Contro, Dalian 116023, Peoples R China
2.Qingdao Natl Lab Marine Sci & Technol, Funct Lab Marine Fisheries Sci & Food Prod Proc, Qingdao 266200, Peoples R China
3.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
4.Dalian Ocean Univ, 52 Heishijiao St, Dalian 116023, Peoples R China
Recommended Citation
GB/T 7714
Yang, Chuanyan,Wang, Lingling,Jia, Zhihao,et al. Two short peptidoglycan recognition proteins from Crassostrea gigas with similar structure exhibited different PAMP binding activity[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2017,70:9-18.
APA Yang, Chuanyan.,Wang, Lingling.,Jia, Zhihao.,Yi, Qilin.,Xu, Qingsong.,...&Song, Linsheng.(2017).Two short peptidoglycan recognition proteins from Crassostrea gigas with similar structure exhibited different PAMP binding activity.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,70,9-18.
MLA Yang, Chuanyan,et al."Two short peptidoglycan recognition proteins from Crassostrea gigas with similar structure exhibited different PAMP binding activity".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 70(2017):9-18.
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