| 缢蛏C型凝集素基因ScCTL-2的序列分析及凝菌活性 |
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| 引用本文： | 蓝天一,牛东红,刘晓军,彭茂潇,李家乐.缢蛏C型凝集素基因ScCTL-2的序列分析及凝菌活性[J].上海海洋大学学报,2019,28(1):20-28. |
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| 作者姓名： | 蓝天一 牛东红 刘晓军 彭茂潇 李家乐 |
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| 作者单位： | 上海海洋大学省部共建水产种质资源发掘与利用教育部重点实验室 |
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| 基金项目： | 国家高技术研究发展计划（2012AA10A400-3）；国家自然科学基金（31472278）；上海知识服务平台（ZF1206） |
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| 摘 要： | 为研究缢蛏C型凝集素基因ScCTL-2的结构和功能特点,克隆了该基因的全长序列,并对其mRNA的表达模式以及重组蛋白的凝菌活性进行研究。结果显示,ScCTL-2的cDNA全长2 194 bp,共编码630个氨基酸,其氨基酸序列拥有4个C型凝集素糖识别结构域和1个N端跨膜区,这一特殊的序列结构不同于任何一种已知的C型凝集素。基因mRNA在健康缢蛏肝胰腺中的表达量显著高于其他组织,在鳃中的表达量次之,而在其余组织中的表达量没有显著性差异;金黄色葡萄球菌与鳗弧菌感染能够显著上调ScCTL-2在缢蛏血细胞中的表达。ScCTL-2的重组蛋白凝菌实验显示:在Ca~(2+)存在的情况下,rScCTL-2能够对实验所采用的金黄色葡萄球菌、枯草芽孢杆菌、大肠杆菌、藤黄微球菌和酿酒酵母均产生明显的凝集反应;当溶液中不存在Ca~(2+)时,凝集反应几乎不能发生,意味着rScCTL-2的凝菌活性是严格Ca~(2+)依赖的。研究表明,ScCTL-2可能是一种新的无脊椎动物C型凝集素类型,它具有无脊椎动物C型凝集素普遍具备的免疫活性,可能在缢蛏的免疫中具有重要作用。
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| 关 键 词： | 缢蛏 C型凝集素 凝菌 |
| 收稿时间： | 2018/4/15 0:00:00 |
| 修稿时间： | 2018/5/15 0:00:00 |
Sequence analysis and bacterial agglutination of C-type lectin gene ScCTL-2 in Sinonovacula constricta |
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| LAN Tianyi,NIU Donghong,LIU Xiaojun,PENG Maoxiao and LI Jiale.Sequence analysis and bacterial agglutination of C-type lectin gene ScCTL-2 in Sinonovacula constricta[J].Journal of Shanghai Ocean University,2019,28(1):20-28. |
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| Authors: | LAN Tianyi NIU Donghong LIU Xiaojun PENG Maoxiao and LI Jiale |
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| Institution: | Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources, Ministry of Education, Shanghai Ocean University, Shanghai 201306, China,Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources, Ministry of Education, Shanghai Ocean University, Shanghai 201306, China,Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources, Ministry of Education, Shanghai Ocean University, Shanghai 201306, China,Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources, Ministry of Education, Shanghai Ocean University, Shanghai 201306, China and Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources, Ministry of Education, Shanghai Ocean University, Shanghai 201306, China |
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| Abstract: | C-type lectins are a superfamily of Ca2+-dependent carbohydrate-binding proteins that play crucial roles in invertebrate immunity. A novel C-type lectin gene (ScCTL-2) was identified in razor clam Sinonovacula constricta. Sequence analysis showed that the full length ScCTL-2 contains a 1893 bp ORF encoding 630 amino acid polypeptide with four CTLD (C-type lectin domain) and a N-terminal transmembrane region. The special structure of ScCTL-2 protein revealed that ScCTL-2 is perhaps a new group of invertebrate C-type lectins. The ScCTL-2 was expressed in almost all tissues, with highest expression in hepatopancreas and the second highest expression in gill. Bacterial stimulation up-regulated ScCTL-2 expression in hemocytes. The spatial-and temporal-specific expression patterns of ScCTL-2 suggest it may be an immune-related gene in razor clam. Recombinant protein (rScCTL-2) displayed a broad bacterial agglutination spectrum, and the agglutinate activity was strictly Ca2+-dependent. It could agglutinate all the experimental bacteria only if Ca2+ existed. The results suggest ScCTL-2 is a novel gene possessing common immune characteristics of invertebrate C-type lectins. |
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| Keywords: | Sinonovacula constricta C-type lectin bacterial agglutination |
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