Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
| The g-type lysozyme of Scophthalmus maximus has a broad substrate spectrum and is involved in the immune response against bacterial infection | |
| Zhao, Lu1,2; Sun, Jin-sheng2; Sun, Li1 | |
| 2011-02-01 | |
| 发表期刊 | FISH & SHELLFISH IMMUNOLOGY
 |
| ISSN | 1050-4648 |
| 卷号 | 30期号:2页码:630-637 |
| 文章类型 | Article |
| 摘要 | Lysozyme is a muramidase that inflicts damage on bacterial cell wall by catalyzing the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan. Lysozymes are classified into several types, one of which is the goose-type (g-type). In this study, we identified and analyzed a g-type lysozyme (SmLysG) from turbot Scophthalmus maximus. The deduced amino acid sequence of SmLysG contains 193 residues and is most closely related to that of the g-type lysozyme of Scophthalmus rhombus (94% overall identity). SmLysG possesses a Goose Egg White Lysozyme (GEWL) domain with conserved residues essential for catalytic activity. Recombinant SmLysG (rSmLysG) purified from yeast exhibits strong lysozyme activity against Micrococcus luteus. Enzyme assays showed that the optimal temperature and pH of rSmLysG are 30 degrees C and pH 7.0, respectively. Substrate spectrum analysis indicated that rSmLysG inhibited the growth of a number of important fish pathogens of both Gram-negative and Gram-positive natures. SmLysG transcription was detected in multiple tissues and was upregulated in kidney and spleen by experimental challenges with lipopolysaccharide and bacterial pathogens that are, respectively, sensitive to and resistant against the lytic effect of rSmLysG. Comparative analysis showed that although bacterial infection also induced the expression of c-type lysozyme, the induction levels were much lower than those of SmLysG. Taken together, these results indicate that SmLysG is a functional g-type lysozyme with a wide working range and is involved in innate immune defense against general bacterial infection. (C) 2011 Elsevier Ltd. All rights reserved.; Lysozyme is a muramidase that inflicts damage on bacterial cell wall by catalyzing the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan. Lysozymes are classified into several types, one of which is the goose-type (g-type). In this study, we identified and analyzed a g-type lysozyme (SmLysG) from turbot Scophthalmus maximus. The deduced amino acid sequence of SmLysG contains 193 residues and is most closely related to that of the g-type lysozyme of Scophthalmus rhombus (94% overall identity). SmLysG possesses a Goose Egg White Lysozyme (GEWL) domain with conserved residues essential for catalytic activity. Recombinant SmLysG (rSmLysG) purified from yeast exhibits strong lysozyme activity against Micrococcus luteus. Enzyme assays showed that the optimal temperature and pH of rSmLysG are 30 degrees C and pH 7.0, respectively. Substrate spectrum analysis indicated that rSmLysG inhibited the growth of a number of important fish pathogens of both Gram-negative and Gram-positive natures. SmLysG transcription was detected in multiple tissues and was upregulated in kidney and spleen by experimental challenges with lipopolysaccharide and bacterial pathogens that are, respectively, sensitive to and resistant against the lytic effect of rSmLysG. Comparative analysis showed that although bacterial infection also induced the expression of c-type lysozyme, the induction levels were much lower than those of SmLysG. Taken together, these results indicate that SmLysG is a functional g-type lysozyme with a wide working range and is involved in innate immune defense against general bacterial infection. (C) 2011 Elsevier Ltd. All rights reserved. |
| 关键词 | G-type Lysozyme Scophthalmus Maximus Bacteriolytic Antimicrobial Innate Immunity |
| 学科领域 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| DOI | 10.1016/j.fsi.2010.12.012 |
| URL | 查看原文 |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000288305300023 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.qdio.ac.cn/handle/337002/11965 |
| 专题 | 实验海洋生物学重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Tianjin Normal Univ, Coll Life Sci, Tianjin 300387, Peoples R China |
| 第一作者单位 | 中国科学院海洋研究所 |
| 推荐引用方式 GB/T 7714 | Zhao, Lu,Sun, Jin-sheng,Sun, Li. The g-type lysozyme of Scophthalmus maximus has a broad substrate spectrum and is involved in the immune response against bacterial infection[J]. FISH & SHELLFISH IMMUNOLOGY,2011,30(2):630-637. |
| APA | Zhao, Lu,Sun, Jin-sheng,&Sun, Li.(2011).The g-type lysozyme of Scophthalmus maximus has a broad substrate spectrum and is involved in the immune response against bacterial infection.FISH & SHELLFISH IMMUNOLOGY,30(2),630-637. |
| MLA | Zhao, Lu,et al."The g-type lysozyme of Scophthalmus maximus has a broad substrate spectrum and is involved in the immune response against bacterial infection".FISH & SHELLFISH IMMUNOLOGY 30.2(2011):630-637. |
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