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Ferritin M of Cynoglossus semilaevis: An iron-binding protein and a broad-spectrum antimicrobial that depends on the integrity of the ferroxidase center and nucleation center for biological activity
Wang, Wei1,2; Zhang, Min1; Sun, Li1
2011-08-01
发表期刊FISH & SHELLFISH IMMUNOLOGY
ISSN1050-4648
卷号31期号:2页码:269-274
文章类型Article
摘要Ferritin is a major intracellular iron storage protein in higher vertebrates and plays an important role in iron metabolism. In this study, we identified and analyzed the biological activity of a ferritin M subunit (CsFerM) from half-smooth tongue sole (Cynoglossus semilaevis). The open reading frame (ORF) of CsFerM is 534 bp and encodes a protein that shares 79.7-86.4% overall sequence identities with the ferritin M subunits of a number of teleosts. In silico analysis identified in CsFerM a eukaryotic ferritin domain with conserved ferroxidase diiron center and ferrihydrite nucleation center. Quantitative real time RT-PCR analysis showed that under normal physiological conditions, expression of CsFerM was highest in liver, moderate in gill, spleen, and muscle, and low in gut, heart, and brain. Following experimental challenge with bacterial pathogens. CsFerM expression was significantly upregulated in kidney, spleen, and liver in time-dependent manners. Biological activity analysis showed that recombinant CsFerM purified from Escherichia coli exhibited apparent iron-binding activity and, when present in the culture medium of six different species of fish bacterial pathogens, completely inhibited bacterial growth. In contrast, a mutant CsFerM that bears alanine substitution at two conserved residues of the ferroxidase diiron center and ferrihydrite nucleation center was abolished in both iron-binding and antimicrobial capacity. These results demonstrate that CsFerM is a biologically active iron chelator with broad-spectrum antibacterial activity, which suggests a role for CsFerM in not only iron storage but also innate immunity. These results also indicate the importance of the conserved iron uptake and mineralization sites to the function of CsFerM. (C) 2011 Elsevier Ltd. All rights reserved.; Ferritin is a major intracellular iron storage protein in higher vertebrates and plays an important role in iron metabolism. In this study, we identified and analyzed the biological activity of a ferritin M subunit (CsFerM) from half-smooth tongue sole (Cynoglossus semilaevis). The open reading frame (ORF) of CsFerM is 534 bp and encodes a protein that shares 79.7-86.4% overall sequence identities with the ferritin M subunits of a number of teleosts. In silico analysis identified in CsFerM a eukaryotic ferritin domain with conserved ferroxidase diiron center and ferrihydrite nucleation center. Quantitative real time RT-PCR analysis showed that under normal physiological conditions, expression of CsFerM was highest in liver, moderate in gill, spleen, and muscle, and low in gut, heart, and brain. Following experimental challenge with bacterial pathogens. CsFerM expression was significantly upregulated in kidney, spleen, and liver in time-dependent manners. Biological activity analysis showed that recombinant CsFerM purified from Escherichia coli exhibited apparent iron-binding activity and, when present in the culture medium of six different species of fish bacterial pathogens, completely inhibited bacterial growth. In contrast, a mutant CsFerM that bears alanine substitution at two conserved residues of the ferroxidase diiron center and ferrihydrite nucleation center was abolished in both iron-binding and antimicrobial capacity. These results demonstrate that CsFerM is a biologically active iron chelator with broad-spectrum antibacterial activity, which suggests a role for CsFerM in not only iron storage but also innate immunity. These results also indicate the importance of the conserved iron uptake and mineralization sites to the function of CsFerM. (C) 2011 Elsevier Ltd. All rights reserved.
关键词Cynoglossus Semilaevis Ferritin Iron Binding Antimicrobial
学科领域Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI10.1016/j.fsi.2011.05.012
URL查看原文
收录类别SCI
语种英语
WOS记录号WOS:000293204500013
引用统计
被引频次:37[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.qdio.ac.cn/handle/337002/11861
专题实验海洋生物学重点实验室
作者单位1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
第一作者单位实验海洋生物学重点实验室
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Wang, Wei,Zhang, Min,Sun, Li. Ferritin M of Cynoglossus semilaevis: An iron-binding protein and a broad-spectrum antimicrobial that depends on the integrity of the ferroxidase center and nucleation center for biological activity[J]. FISH & SHELLFISH IMMUNOLOGY,2011,31(2):269-274.
APA Wang, Wei,Zhang, Min,&Sun, Li.(2011).Ferritin M of Cynoglossus semilaevis: An iron-binding protein and a broad-spectrum antimicrobial that depends on the integrity of the ferroxidase center and nucleation center for biological activity.FISH & SHELLFISH IMMUNOLOGY,31(2),269-274.
MLA Wang, Wei,et al."Ferritin M of Cynoglossus semilaevis: An iron-binding protein and a broad-spectrum antimicrobial that depends on the integrity of the ferroxidase center and nucleation center for biological activity".FISH & SHELLFISH IMMUNOLOGY 31.2(2011):269-274.
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