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| Modification of a synthetic LPS-binding domain of anti-lipopolysaccharide factor from shrimp reveals strong structure-activity relationship in their antimicrobial characteristics | |
Guo, Shuyue1,2; Li, Shihao1; Li, Fuhua1; Zhang, Xiaojun1; Xiang, Jianhai1 ; Li, FH (reprint author), Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, 7 Nanhai Rd, Qingdao 266071, Peoples R China.
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| 2014-08-01 | |
| 发表期刊 | DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
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| 卷号 | 45期号:2页码:227-232 |
| 文章类型 | Article |
| 摘要 | Anti-lipopolysaccharide factor (ALF) is a small protein with broad-spectrum antimicrobial activities and certain antiviral property. Its putative lipopolysaccharide (LPS) binding domain was deduced to be important for its activities. However, there is still no report revealing how the structure of the LPS-binding domain affects its biological function until now. In the present study, we designed and synthesized a peptide corresponding to the LPS-binding domain of ALF from the Chinese shrimp (designated as FcALF-LBDc) and its structure-modified isoforms in order to analyze the relationship between its structure and antimicrobial activities. Results showed that FcALF-LBDc exhibited apparent antibacterial activities against both Gram-negative bacteria Escherichia coli and Vibrio anguillarum and Gram-positive bacteria Micrococcus luteus and Micrococcus lysodeikticus with MIC ranges of 32-64, 2-4, 1-2, and 32-64 mu M, respectively. The disulfide loop and the basic amino acids in the LPS-binding domain (LBD) of ALF played key roles in its antibacterial activities. In addition, FcALF-LBDc could reduce the propagation of white spot syndrome virus (WSSV) in vivo, and its lysine residue is indispensable for its antiviral property. This is the first attempt to testify the effects of the sequence features of the LPS-binding domain on its antimicrobial activities. (C) 2014 Elsevier Ltd. All rights reserved. |
| 关键词 | Antibacterial Alf Antiviral Lps-binding Domain Shrimp |
| 学科领域 | Immunology ; Zoology |
| DOI | 10.1016/j.dci.2014.03.003 |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000337856600006 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.qdio.ac.cn/handle/337002/24128 |
| 专题 | 实验海洋生物学重点实验室 |
| 通讯作者 | Li, FH (reprint author), Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, 7 Nanhai Rd, Qingdao 266071, Peoples R China. |
| 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 |
| 第一作者单位 | 实验海洋生物学重点实验室 |
| 推荐引用方式 GB/T 7714 | Guo, Shuyue,Li, Shihao,Li, Fuhua,et al. Modification of a synthetic LPS-binding domain of anti-lipopolysaccharide factor from shrimp reveals strong structure-activity relationship in their antimicrobial characteristics[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2014,45(2):227-232. |
| APA | Guo, Shuyue,Li, Shihao,Li, Fuhua,Zhang, Xiaojun,Xiang, Jianhai,&Li, FH .(2014).Modification of a synthetic LPS-binding domain of anti-lipopolysaccharide factor from shrimp reveals strong structure-activity relationship in their antimicrobial characteristics.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,45(2),227-232. |
| MLA | Guo, Shuyue,et al."Modification of a synthetic LPS-binding domain of anti-lipopolysaccharide factor from shrimp reveals strong structure-activity relationship in their antimicrobial characteristics".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 45.2(2014):227-232. |
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