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从褐菖鲉(Sebastes schlegeli)中克隆和鉴定肽聚糖识别蛋白。

Molecular cloning and characterization of peptidoglycan recognition proteins from the rockfish, Sebastes schlegeli.

机构信息

Department of Biology, Research Institute of Life Science, Gyeongsang National University, 900 Gajwa-dong, Jinju 660-701, Republic of Korea.

出版信息

Fish Shellfish Immunol. 2010 Apr;28(4):632-9. doi: 10.1016/j.fsi.2009.12.023. Epub 2010 Jan 1.

DOI:10.1016/j.fsi.2009.12.023
PMID:20045065
Abstract

Peptidoglycan recognition proteins (PGRPs) are innate immune molecules that are structurally conserved through evolution in both invertebrate and vertebrate animals. Here we report the identification and characterization of two long forms of PGRP (SsPGRP-L1 and SsPGRP-L2) from the rockfish, Sebastes schlegeli. The deduced amino acid sequences of SsPGRP-L1 and SsPGRP-L2, 466 and 482 residues respectively, contain the conserved PGRP domain and the four Zn(2+)-binding amino acid residues required for amidase activity. In addition to peptidoglycan-lytic amidase activity, recombinant SsPGRPs have broad-spectrum antimicrobial activity like zebrafish PGRPs. RT-PCR analysis of total RNA shows that the expression patterns of SsPGRP-L1 and SsPGRP-L2 genes are different, though they are widely expressed in the tissues that come in contact with bacteria. Overall, these data suggest that rockfish PGRPs are involved in the innate host defense of S. schlegeli against bacterial infections.

摘要

肽聚糖识别蛋白(PGRPs)是结构保守的先天免疫分子,在无脊椎动物和脊椎动物中通过进化得到了保守。本研究从褐菖鲉(Sebastes schlegeli)中鉴定并描述了两种长型 PGRP(SsPGRP-L1 和 SsPGRP-L2)。SsPGRP-L1 和 SsPGRP-L2 的推导氨基酸序列分别为 466 和 482 个残基,包含保守的 PGRP 结构域和 4 个锌(Zn2+)结合残基,这些残基对于 amidase 活性是必需的。除了肽聚糖裂解酰胺酶活性外,重组 SsPGRPs 与斑马鱼 PGRPs 一样具有广谱的抗菌活性。总 RNA 的 RT-PCR 分析表明,尽管 SsPGRP-L1 和 SsPGRP-L2 基因在与细菌接触的组织中广泛表达,但它们的表达模式不同。总的来说,这些数据表明褐菖鲉 PGRPs 参与了 S. schlegeli 对细菌感染的先天宿主防御。

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