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首页> 外文期刊>Fish & Shellfish Immunology >Molecular cloning and characterization of cathepsin L from freshwater mussel, Cristaria plicata
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Molecular cloning and characterization of cathepsin L from freshwater mussel, Cristaria plicata

机译：淡水贻贝Cristaria plicata组织蛋白酶L的分子克隆和表征

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Cathepsin L is one of the crucial enzyme superfamilies and involved in the immune responses. The Cathepsin L cDNA and genome of Cristaria plicata (CpCL) was cloned from the hemocytes using degenerate primers by the rapid amplification of cDNA ends (RACE) PCR. The genomic DNA was 9353 bp long and had a total of six introns and seven exons. The full-length cDNA of CpCL was 1144 bp, the cDNA contained a 5' untranslated region (UTR) of 34 nucleotides, the 3' UTR of 108 bp with a canonical polyadenylation signal sequence AATAAA and a polyA tail, and an open reading frame (ORF) of 1002 bp, encoding 333 amino acid residues with 37.65 kDa predicted molecular weight. The theoretical isoelectric point was 8.61. The prepro-cathepsin L was consisted of a typical signal peptide (Met1-Gly20), a pro-region peptide (Leu21-Glu116) and a mature peptide (Tyr117-Val333). Many members of the papain family possessed of a proline residue at position 2 in the mature enzymem, this was also observed in CpCL. The preproprotein included an oxyanion hole (Gln 135), the active center formed by Cys141, His280 and Asn 300, the potential N-glycosylation site (Asn38, Asn 113 and Asn 272) and the conserved GCXGG motifs, which was characteristic of cathepsin, the conserved ERWNIN and GNFD motifs, which were characteristic for cathepsin L. Homology analysis revealed that the CpCL shared 49-87% identity to other known cathepsin L sequences. The phylogenetic tree showed that the CpCL clustered with the invertebrate cathepsin L cysteine proteases, and was closely related to the cathepsin L of Hyriopsis cumingii. The expression of CpCL mRNA was detected in hepatopancreas, hemocytes, mantle, gills and adductor muscle, Mid the higher expression level was in hepatopancreas. After A. hydrophila stimulation, the expression of the CpCL mRNA was up-regulated in hemocytes and hepatopancreas, and the expression level was significantly lower in gill than one after PBS challenge group
机译：组织蛋白酶L是至关重要的酶超家族之一，并参与免疫反应。通过简并引物通过快速扩增cDNA末端（RACE）PCR从血细胞克隆组织蛋白酶L cDNA和Cristaria plicata的基因组（CpCL）。基因组DNA长9353 bp，共有六个内含子和七个外显子。 CpCL的全长cDNA为1144 bp，cDNA包含34个核苷酸的5'非翻译区（UTR），108 bp的3'UTR，具有规范的聚腺苷酸化信号序列AATAAA和polyA尾巴，以及一个开放阅读框（ORF）为1002 bp，编码333个氨基酸残基，预测分子量为37.65 kDa。理论等电点为8.61。蛋白酶原L由典型的信号肽（Met1-Gly20），前区肽（Leu21-Glu116）和成熟肽（Tyr117-Val333）组成。木瓜蛋白酶家族的许多成员在成熟酶的2位具有脯氨酸残基，这在CpCL中也观察到。前蛋白原包括一个氧阴离子孔（Gln 135），由Cys141，His280和Asn 300形成的活性中心，潜在的N-糖基化位点（Asn38，Asn 113和Asn 272）和保守的GCXGG基序，这是组织蛋白酶的特征，保守的ERWNIN和GNFD基序是组织蛋白酶L的特征。同源性分析显示CpCL与其他已知的组织蛋白酶L序列具有49-87％的同一性。系统发育树表明，CpCL与无脊椎动物组织蛋白酶L的半胱氨酸蛋白酶成簇，并且与三角帆蚌的组织蛋白酶L密切相关。 CpCL mRNA的表达在肝胰腺，血细胞，地幔，g和内收肌中均有表达，中度表达在肝胰腺中。嗜水链球菌刺激后，血细胞和肝胰腺中CpCL mRNA的表达上调，g的表达水平明显低于PBS攻击组。

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