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首页> 外文期刊>Fish & Shellfish Immunology >Identification and expression analysis on bactericidal permeability-increasing protein (BPI)/lipopolysaccharide-binding protein (LBP) of ark shell, Scapharca broughtonii
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Identification and expression analysis on bactericidal permeability-increasing protein (BPI)/lipopolysaccharide-binding protein (LBP) of ark shell, Scapharca broughtonii

机译：方舟S鱼杀菌通透性增强蛋白/脂多糖结合蛋白的鉴定与表达分析

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摘要

Bactericidal permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP) are the numbers of the lipid transfer protein/lipopolysaccharide-binding protein family and play crucial roles in the innate immune response to Gram-negative bacteria. A novel Sb-BPI/LBP1 from ark shell Scapharca broughtonii was isolated by expressed sequence tag (EST) and RACE techniques. The Sb-BPI/LBP1 cDNA encoded a polypeptide of 484 amino acids with a putative signal peptide of 21 amino acid residues and a mature protein of 463 amino acids. The deduced amino acid sequence of Sb-BPI/LBP1 contained an N-terminal BPI/LBP/CETP domain BPI1 with three functional regions that display LPS-binding activity, and a C-terminal BPI/LBP/CETP domain BPI2. In structure and sequence, Sb-BPI/LBP1 showed highly similar to those of the BPI/LBPs from invertebrate and non-mammalian vertebrate, the LBPs and BPIs from mammal. By quantitative real-time RT-PCR, Sb-BPI/LBP1 transcripts could be detected in all normal tested tissues, including hepatopancreas, adductor muscle, mantle margin, heart, gonad, gill and hemocytes, and was universally up-regulatable at 24 h post LPS challenge. The mRNA expression of Sb-BPI/LBP1 in hemocytes was the most sensitive to LPS challenge, significantly up-regulated at 12 h post LPS challenge and peaked at 24 h (16.76-fold, P < 0.05). These results suggested that Sb-BPI/LBP1 was a constitutive and inducible acute-phase protein contributing to the host immune defense against Gram-negative bacterial infection in ark shell S. broughtonii. (C) 2013 Elsevier Ltd. All rights reserved.
机译：杀菌通透性增加蛋白（BPI）和脂多糖结合蛋白（LBP）是脂质转移蛋白/脂多糖结合蛋白家族的数目，并且在对革兰氏阴性细菌的先天免疫应答中起关键作用。通过表达序列标签（EST）和RACE技术分离了方舟壳cap鱼的新型Sb-BPI / LBP1。 Sb-BPI / LBP1 cDNA编码了484个氨基酸的多肽，推定的信号肽为21个氨基酸残基，成熟蛋白为463个氨基酸。推导的Sb-BPI / LBP1氨基酸序列包含一个具有三个显示LPS结合活性的功能区的N端BPI / LBP / CETP域BPI1和一个C端BPI / LBP / CETP域BPI2。在结构和序列上，Sb-BPI / LBP1与无脊椎动物和非哺乳动物脊椎动物的BPI / LBP，哺乳动物的LBP和BPI高度相似。通过实时定量RT-PCR，可以在所有正常测试的组织中检测到Sb-BPI / LBP1转录本，包括肝胰腺，内收肌，套层边缘，心脏，性腺，g和血细胞，并且在24 h普遍上调LPS挑战后。血细胞中Sb-BPI / LBP1的mRNA表达对LPS攻击最敏感，在LPS攻击后12 h明显上调，在24 h达到峰值（16.76倍，P <0.05）。这些结果表明，Sb-BPI / LBP1是一种组成型和诱导型急性期蛋白，有助于宿主抵抗带壳贝氏酵母中革兰氏阴性细菌的感染。 （C）2013 Elsevier Ltd.保留所有权利。

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