A peptidoglycan recognition protein from Sciaenops ocellatus is a zinc amidase and a bactericide with a substrate range limited to Gram-positive bacteria
文献类型：期刊论文
| 作者 | Li, Mo-Fei1,2 ; Zhang, Min2; Wang, Chun-Lin1; Sun, Li2
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| 刊名 | FISH & SHELLFISH IMMUNOLOGY
 |
| 出版日期 | 2012-02-01 |
| 卷号 | 32期号:2页码:322-330 |
| 关键词 | Peptidoglycan recognition protein Amidase Sciaenops ocellatus Bactericide |
| ISSN号 | 1050-4648 |
| 通讯作者 | Sun, L (reprint author), Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, 7 Nanhai Rd, Qingdao 266071, Peoples R China. |
| 英文摘要 | Peptidoglycan recognition proteins (PGRPs) are a family of innate immune molecules that recognize bacterial peptidoglycan. PGRPs are highly conserved in invertebrates and vertebrates including fish. However, the biological function of teleost PGRP remains largely uninvestigated. In this study, we identified a PGRP homologue, SoPGLYRP-2, from red drum (Sciaenops ocellatus) and analyzed its activity and potential function. The deduced amino acid sequence of SoPGLYRP-2 is composed of 482 residues and shares 46-94% overall identities with known fish PGRPs. SoPGLYRP-2 contains at the C-terminus a single zinc amidase domain with conserved residues that form the catalytic site. Quantitative RT-PCR analysis detected SoPGLYRP-2 expression in multiple tissues, with the highest expression occurring in liver and the lowest expression occurring in brain. Experimental bacterial infection upregulated SoPGLYRP-2 expression in kidney, spleen, and liver in time-dependent manners. To examine the biological activity of SoPGLYRP-2, purified recombinant proteins representing the intact SoPGLYRP-2 (rSoPGLYRP-2) and the amidase domain (rSoPGLYRP-AD) were prepared from Escherichia coli. Subsequent analysis showed that rSoPGLYRP-2 and rSoPGLYRP-AD (i) exhibited comparable Zn2+-dependent peptidoglycanlytic activity and were able to recognize and bind to live bacterial cells, (ii) possessed bactericidal effect against Gram-positive bacteria and slight bacteriostatic effect against Gram-negative bacteria, (iii) were able to block bacterial infection into host cells. These results indicate that SoPGLYRP-2 is a zinc-dependent amidase and a bactericide that targets preferentially at Gram-positive bacteria, and that SoPGLYRP-2 is likely to play a role in host innate immune defense during bacterial infection. (C) 2011 Elsevier Ltd. All rights reserved. |
| 学科主题 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 收录类别 | SCI |
| 原文出处 | 10.1016/j.fsi.2011.11.024 |
| 语种 | 英语 |
| WOS记录号 | WOS:000300751800011 |
| 公开日期 | 2013-09-24 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/12266]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 作者单位 | 1.Ningbo Univ, Ningbo 315211, Zhejiang, Peoples R China 2.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China |
| 推荐引用方式 GB/T 7714 | Li, Mo-Fei,Zhang, Min,Wang, Chun-Lin,et al. A peptidoglycan recognition protein from Sciaenops ocellatus is a zinc amidase and a bactericide with a substrate range limited to Gram-positive bacteria[J]. FISH & SHELLFISH IMMUNOLOGY,2012,32(2):322-330. |
| APA | Li, Mo-Fei,Zhang, Min,Wang, Chun-Lin,&Sun, Li.(2012).A peptidoglycan recognition protein from Sciaenops ocellatus is a zinc amidase and a bactericide with a substrate range limited to Gram-positive bacteria.FISH & SHELLFISH IMMUNOLOGY,32(2),322-330. |
| MLA | Li, Mo-Fei,et al."A peptidoglycan recognition protein from Sciaenops ocellatus is a zinc amidase and a bactericide with a substrate range limited to Gram-positive bacteria".FISH & SHELLFISH IMMUNOLOGY 32.2(2012):322-330. |
入库方式： OAI收割
来源：海洋研究所
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