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首页> 外文期刊>Fish & Shellfish Immunology >Molecular properties and immune defense of two ferritin subunits from freshwater pearl mussel, Hyriopsis schlegelii.
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Molecular properties and immune defense of two ferritin subunits from freshwater pearl mussel, Hyriopsis schlegelii.

机译：淡水珍珠贻贝Hyriopsis schlegelii的两个铁蛋白亚基的分子特性和免疫防御。

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摘要

Ferritin is a conserved iron-binding protein involved in cellular iron metabolism and host defense. In the present study, two distinct cDNAs for ferritins in the freshwater pearl mussel Hyriopsis schlegelii were identified (designated as HsFer-1 and HsFer-2) by SMART RACE approach and expressed sequence tag (EST) analysis. The full-length cDNAs of HsFer-1 and HsFer-2 were of 760 and 877 bp, respectively. Both of the two cDNAs contained an open reading frame (ORF) of 522 bp encoding for 174 amino acid residues. Sequence characterization and homology alignment indicated that HsFer-1 and HsFer-2 had higher similarity to H-type subunit of vertebrate ferritins than L-type subunit. Analysis of the HsFer-1 and HsFer-2 untranslated regions (UTR) showed that both of them had an iron response element (IRE) in the 5'-UTR, which was considered to be the binding site for iron regulatory protein (IRP). Quantitative real-time PCR (qPCR) assays were employed to examine the mRNA expression profiles. Under normal physiological conditions, the expression level of both HsFer-1 and HsFer-2 mRNA were the highest in hepatopancreas, moderate in gonad, axe foot, intestine, kidney, heart, gill, adductor muscle and mantle, the lowest in hemocytes. After stimulation with bacteria Aeromonas hydrophila, HsFer-1 mRNA experienced a different degree of increase in the tissues of hepatopancreas, gonad and hemocytes, the peak level was 2.47-fold, 9.59-fold and 1.37-fold, respectively. Comparatively, HsFer-2 showed up-regulation in gonad but down-regulation in hepatopancreas and hemocytes. Varying expression patterns indicate that two types of ferritins in H. schlegelii might play different roles in response to bacterial challenge. Further bacteriostatic analysis showed that both the purified recombinant ferritins inhibited the growth of A. hydrophila to a certain degree. Collectively, our results suggest that HsFer-1 and HsFer-2 are likely to be functional proteins involved in immune defense against bacterial infection.
机译：铁蛋白是一种参与细胞铁代谢和宿主防御的保守的铁结合蛋白。在本研究中，通过SMART RACE方法鉴定了淡水珍珠蚌贻贝（Hyriopsis schlegelii）中铁蛋白的两个不同cDNA（分别称为HsFer-1和HsFer-2），并表达了序列标签（EST）分析。 HsFer-1和HsFer-2的全长cDNA分别为760和877 bp。这两个cDNA均包含522 bp的开放阅读框（ORF），编码174个氨基酸残基。序列特征和同源性比对表明，HsFer-1和HsFer-2与脊椎动物铁蛋白的H型亚基的相似性高于L型亚基。对HsFer-1和HsFer-2非翻译区（UTR）的分析表明，它们两者在5'-UTR中均具有铁反应元件（IRE），这被认为是铁调节蛋白（IRP）的结合位点。定量实时PCR（qPCR）分析用于检查mRNA表达谱。在正常生理条件下，HsFer-1和HsFer-2 mRNA的表达水平在肝胰腺中最高，在性腺，斧脚，肠，肾，心脏，g，内收肌和地幔中中等，在血细胞中最低。细菌嗜水气单胞菌刺激后，HsFer-1 mRNA在肝胰腺，性腺和血细胞组织中出现不同程度的增加，其峰值分别为2.47倍，9.59倍和1.37倍。比较而言，HsFer-2在性腺中显示上调，但在肝胰腺和血细胞中显示下调。不同的表达模式表明，施氏嗜血杆菌中的两种类型的铁蛋白可能在响应细菌攻击中发挥不同的作用。进一步的抑菌分析表明，两种纯化的重组铁蛋白均在一定程度上抑制了嗜水链球菌的生长。总的来说，我们的结果表明，HsFer-1和HsFer-2可能是参与针对细菌感染的免疫防御的功能蛋白。

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