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A GTP-dependent Phosphoenolpyruvate Carboxykinase from Crassostrea gigas Involved in Immune Recognition
Lv, Zhao1,2,3; Qiu, Limei1; Wang, Weilin1,3; Liu, Zhaoqun1,3; Xue, Zhuang4; Yu, Zichao4; Song, Xiaorui4; Chen, Hao1,3; Wang, Lingling2,4; Song, Linsheng2,4
2017-12-01
Source PublicationDEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume77Pages:318-329
SubtypeArticle
AbstractPhosphoenolpyruvate carboxykinase (PEPCK) is well known as a key enzyme involved in the metabolic pathway of gluconeogenesis in organisms, but the information about its involvement in immune response is still very limited. In the present study, a novel PEPCK homolog named CgPEPCIC was identified from oyster Crassostrea gigas. The deduced amino acid sequence of CgPEPCK shared 52%-74% similarities with those from other known PEPCKs. There were one conserved guanosine triphosphate (GTP) binding site, one substrate binding site, one metal binding site and one active site in CgPEPCK. The mRNA transcripts of CgPEPCK were constitutively expressed in all the tested tissues including hemolymph, mantle, gill, muscle, gonad and hepatopancreas. CgPEPCK proteins were mainly distributed in adductor muscle, gonad, gill and mantle, and rarely detected in hepatopancreas by using immunohistochemical analysis. After the stimulations with lipopolysaccharide (LPS), peptidoglycan (PGN), Vibrio splendidus and V. anguillarum, CgPEPCK transcripts in hemocytes were significantly up-regulated and peaked at 6 h (LPS, 9.62-fold, p < 0.01), 9 h (PGN, 4.25-fold, p < 0.01), 12 h (V. splendidus, 5.72-fold, p < 0.01), 3 h (V. anguillarum, 2.87-fold, p < 0.01), respectively. The recombinant CgPEPCK protein (rCgPEPCK) exhibited Mn2+/Mg2+ dependent GTP binding activity, and the activities to bind LPS and PGN, but not beta-1,3-glucan (GLU), lipoteichoic acid (LTA), mannan (MAN) nor polyinosinic-polycytidylic (Poly I: C). It could also bind Escherichia coli, Staphylococcus aureus, Micrococcus luteus and significantly inhibit their growth. All these results collectively suggested that CgPEPCK could not only exert GTP binding activity involved in gluconeogenesis, but also mediate the bacteria recognition and clearance in, immune response of oysters. (C) 2017 Elsevier Ltd. All rights reserved.
KeywordPhosphoenolpyruvate Carboxykinase Gtp Binding Activity Immune Responses Pamp Binding Activity
DOI10.1016/j.dci.2017.09.001
Indexed BySCI
Language英语
WOS IDWOS:000413387100034
Citation statistics
Document Type期刊论文
Version出版稿
Identifierhttp://ir.qdio.ac.cn/handle/337002/143242
Collection实验海洋生物学重点实验室
Affiliation1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Fisheries Sci & Food Prod Proc, Qingdao 266071, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.Dalian Ocean Univ, Liaoning Key Lab Marine Anim Immunol & Dis Contro, Dalian 116023, Peoples R China
First Author Affilication中国科学院海洋研究所
Recommended Citation
GB/T 7714
Lv, Zhao,Qiu, Limei,Wang, Weilin,et al. A GTP-dependent Phosphoenolpyruvate Carboxykinase from Crassostrea gigas Involved in Immune Recognition[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2017,77:318-329.
APA Lv, Zhao.,Qiu, Limei.,Wang, Weilin.,Liu, Zhaoqun.,Xue, Zhuang.,...&Song, Linsheng.(2017).A GTP-dependent Phosphoenolpyruvate Carboxykinase from Crassostrea gigas Involved in Immune Recognition.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,77,318-329.
MLA Lv, Zhao,et al."A GTP-dependent Phosphoenolpyruvate Carboxykinase from Crassostrea gigas Involved in Immune Recognition".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 77(2017):318-329.
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