Characterization of a c-type lysozyme of Scophthalmus maximus: Expression, activity, and antibacterial effect
文献类型：期刊论文
| 作者 | Yu, Lan-ping1,2; Sun, Bo-guang1 ; Li, Jun1,3; Sun, Li1
|
| 刊名 | FISH & SHELLFISH IMMUNOLOGY
 |
| 出版日期 | 2013 |
| 卷号 | 34期号:1页码:46-54 |
| 关键词 | c-Type lysozyme Scophthalmus maximus Bacteriolytic Catalytic site |
| ISSN号 | 1050-4648 |
| 通讯作者 | Sun, L |
| 中文摘要 | Lysozyme is a key component of the innate immune system and plays an important role in antibacterial infection. In this study, we analyzed the expression and activity of a chicken-type (c-type) lysozyme (named SmLysC) from turbot (Scophthalmus maximus). SmLysC is composed of 143 residues and shares 67-90% overall sequence identities with the c-type lysozymes of a number of teleost fish. SmLysC possesses a typical c-type lysozyme domain, which contains the conserved residues E50 and D67 that form the putative catalytic site. SmLysC expression was detected, in increasing order, in head kidney, gill, heart, muscle, brain, spleen, blood, and liver. Bacterial infection caused significant inductions of SmLysC expression in head kidney, spleen, and liver in a time-dependent manner. Immunoblot analysis indicated that SmLysC has a subcellular localization in the extracellular milieu. Recombinant SmLysC (rSmLysC) was able to bind to bacterial cells and inhibit bacterial growth. Enzyme assay showed that the optimal temperature and pH of rSmLysC were 37 degrees C and pH 6.0 respectively. In contrast to rSmLysC, the mutant protein rSmLysCM1, which bears alanine substitutions at E50 and D67, displayed drastically reduced bacteriolytic activity. rSmLysC was able to inhibit the growth of several fish bacterial pathogens in a manner that depended on the dose of the protein; however, Gram-positive bacteria were in general more sensitive to rSmLysC than Gram-negative bacteria. Together these results indicate that SmLysC is a functional lysozyme that is likely to participate in innate immune defense against extracellular bacterial pathogens, in particular those of Gram-positive nature. (c) 2012 Elsevier Ltd. All rights reserved. |
| 英文摘要 | Lysozyme is a key component of the innate immune system and plays an important role in antibacterial infection. In this study, we analyzed the expression and activity of a chicken-type (c-type) lysozyme (named SmLysC) from turbot (Scophthalmus maximus). SmLysC is composed of 143 residues and shares 67-90% overall sequence identities with the c-type lysozymes of a number of teleost fish. SmLysC possesses a typical c-type lysozyme domain, which contains the conserved residues E50 and D67 that form the putative catalytic site. SmLysC expression was detected, in increasing order, in head kidney, gill, heart, muscle, brain, spleen, blood, and liver. Bacterial infection caused significant inductions of SmLysC expression in head kidney, spleen, and liver in a time-dependent manner. Immunoblot analysis indicated that SmLysC has a subcellular localization in the extracellular milieu. Recombinant SmLysC (rSmLysC) was able to bind to bacterial cells and inhibit bacterial growth. Enzyme assay showed that the optimal temperature and pH of rSmLysC were 37 degrees C and pH 6.0 respectively. In contrast to rSmLysC, the mutant protein rSmLysCM1, which bears alanine substitutions at E50 and D67, displayed drastically reduced bacteriolytic activity. rSmLysC was able to inhibit the growth of several fish bacterial pathogens in a manner that depended on the dose of the protein; however, Gram-positive bacteria were in general more sensitive to rSmLysC than Gram-negative bacteria. Together these results indicate that SmLysC is a functional lysozyme that is likely to participate in innate immune defense against extracellular bacterial pathogens, in particular those of Gram-positive nature. (c) 2012 Elsevier Ltd. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 学科主题 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 类目[WOS] | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 研究领域[WOS] | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 关键词[WOS] | GOOSE-TYPE LYSOZYME ; MOLECULAR CHARACTERIZATION ; IMMUNOPROTECTIVE ANALYSIS ; VACCINE CANDIDATE ; CDNA ; IDENTIFICATION ; PHYLOGENY ; INFECTION ; PATTERN ; ANTIGEN |
| 收录类别 | SCI |
| 原文出处 | 10.1016/j.fsi.2012.10.007 |
| 语种 | 英语 |
| WOS记录号 | WOS:000314743600006 |
| 公开日期 | 2014-07-17 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/16538]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 3.Lake Super State Univ, Sch Biol Sci, Sault Ste Marie, MI USA |
| 推荐引用方式 GB/T 7714 | Yu, Lan-ping,Sun, Bo-guang,Li, Jun,et al. Characterization of a c-type lysozyme of Scophthalmus maximus: Expression, activity, and antibacterial effect[J]. FISH & SHELLFISH IMMUNOLOGY,2013,34(1):46-54. |
| APA | Yu, Lan-ping,Sun, Bo-guang,Li, Jun,&Sun, Li.(2013).Characterization of a c-type lysozyme of Scophthalmus maximus: Expression, activity, and antibacterial effect.FISH & SHELLFISH IMMUNOLOGY,34(1),46-54. |
| MLA | Yu, Lan-ping,et al."Characterization of a c-type lysozyme of Scophthalmus maximus: Expression, activity, and antibacterial effect".FISH & SHELLFISH IMMUNOLOGY 34.1(2013):46-54. |
入库方式： OAI收割
来源：海洋研究所
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