| 鹿角杯形珊瑚溶菌酶PdLYZ重组蛋白的表达及其体外抑菌活性特征 |
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| 引用本文： | 唐佳,倪兴振,邢皓程,王佑笑,杨倩曦,闫智聪,周智,赵建民.鹿角杯形珊瑚溶菌酶PdLYZ重组蛋白的表达及其体外抑菌活性特征[J].热带生物学报,2021,12(2):139-146. |
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| 作者姓名： | 唐佳 倪兴振 邢皓程 王佑笑 杨倩曦 闫智聪 周智 赵建民 |
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| 作者单位： | 中国科学院烟台海岸带研究所,山东烟台 264003;中国科学院大学,北京 100049;海南大学海洋学院,海口 570228;海南华侨中学,海口 570226;中国科学院烟台海岸带研究所,山东烟台 264003 |
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| 基金项目： | 国家重点研发计划（2018YFC1406500）；国家自然科学基金（31772460）；海南省自然科学基金（2019RC067） |
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| 摘 要： | 珊瑚疾病的大规模爆发已严重威胁到珊瑚礁生态系统的结构和功能。溶菌酶是无脊椎动物固有免疫应答中的重要效应分子之一。本研究从鹿角杯形珊瑚（Pocillopora damicornis）中克隆得到了1个溶菌酶基因（PdLYZ），随后体外诱导表达并纯化PdLYZ重组蛋白，同时测定PdLYZ重组蛋白对大肠杆菌（Escherichia coli）、变异链球菌（Streptococcus mutans）和溶珊瑚弧菌（Vibrio coralliilyticus）的抑菌活性，还探究了PdLYZ重组蛋白在高温条件下对病原菌溶珊瑚弧菌抑制活性变化。研究结果:PdLYZ的cDNA开放阅读框长648 bp，编码215个氨基酸残基，其序列与其他生物的溶菌酶相似性为25.54%～49.15%；生物信息学预测PdLYZ推导蛋白具有1个类溶菌酶超家族结构域（Ile31-Gly214）；PdLYZ重组蛋白能显著抑制大肠杆菌、变异链球菌和溶珊瑚弧菌的生长；PdLYZ重组蛋白在高温条件下会在前期显著抑制溶珊瑚弧菌的生长。这些结果表明，溶菌酶PdLYZ可能参与珊瑚免疫防御。本研究为进一步理解珊瑚免疫机制提供了理论参考。
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| 关 键 词： | 鹿角杯形珊瑚 溶菌酶 原核表达 抗菌活性 |
| 收稿时间： | 2020-10-01 |
Recombinant Protein Expression and Bacteriostatic Activity of Pocillopora damicornis Lysozyme in Vitro |
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| Affiliation: | 1.Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai, Shandong 264003, China2.University of Chinese Academy of Sciences, Beijing 100049, China3.College of Marine Sciences, Hainan University, Haikou, Hainan 570228, China4.Hainan Overseas Chinese Middle School, Haikou, Hainan 570226, China |
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| Abstract: | Large-scale outbreaks of coral diseases have been seriously threatening the health of coral reef ecosystems. Lysozyme is one of the important effectors in the innate immune response of invertebrates. A lysozyme gene, PdLYZ, was cloned from Pocillopora damicornis. The recombinant protein of PdLYZ (rPdLYZ) was expressed and purified in vitro, and its bacteriostatic activities against the Gram-positive bacteria Streptococcus mutans and Gram-negative bacteria Escherichia coli were determined. The effect of high temperature on the bacteriostatic activity of rPdLYZ against the pathogenic bacteria Vibrio coralliilyticus was further explored. The identified PdLYZ was comprised of 215 amino acid residues and predicted to contain one lysozyme-like superfamily domain (Ile31-Gly214), and its sequence was 25.54%?49.15% similar to those of lysozymes from other organisms. Results showed that rPdLYZ had lytic activities against E. coli, S. mutans and V. coralliilyticus. The rPdLYZ inhibited the growth of V. coralliilyticus at the early stage under high temperature. These results suggest that PdLYZ be involved in the immune defense of corals, and this study provides a theoretical reference for further understanding of the immune mechanism of corals. |
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