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TC38, a teleost TFPI-2 peptide that kills bacteria via penetration of the cell membrane and interaction with nucleic acids

文献类型： 外文期刊

作者： Zhang, Min 1 ; Yue, Bin 1 ; Zhang, Ai-hua 3 ; Wang, Guang-hua 1 ; Liu, Yong 1 ; Zhou, Shun 1 ; Cheng, Shun-feng 1 ; Li, N 1 ;

作者机构： 1.Qingdao Agr Univ, Marine Sci & Engn Coll, Qingdao 266109, Peoples R China

2.Chinese Acad Fishery Sci, Pearl River Fisheries Res Inst, Key Lab Aquat Anim Immune Technol, Key Lab Fishery Drug Dev,Minist Agr, Guangzhou 510380, Guangdong, Peoples R China

3.Shandong Univ, Qilu Hosp, Anim Lab, Jinan 250012, Peoples R China

关键词： Tongue sole;TFPI-2;Antimicrobial peptide;Antibacterial activity

期刊名称：FISH & SHELLFISH IMMUNOLOGY （ 影响因子：4.581； 五年影响因子：4.851 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： Tissue factor pathway inhibitor 2 (TFPI-2) is an analog of TFPI-1 and a potent endogenous inhibitor of tissue factor (TF)-mediated blood coagulation. Recent reports have proven that the C-terminal of TFPI-2 peptides in humans and several other vertebrates possesses antibacterial activity against Gram-positive and Gram-negative bacteria. In our previous study, we reported that the TFPI-2 peptide, TC38 in tongue sole (Cynoglossus semilaevis) was active against Micrococcus luteus. In this study, we further examine the antimicrobial spectrum, mechanism of action, and function of TC38 in tongue sole. Our results indicate that TC38 is active against the Gram-negative bacteria Vibrio ichthyoenteri, Vibrio litoralis, Vibrio parahaemolyticus, and Vibrio vulnificus, as well as the fish Megalocytivirus, infectious spleen and kidney necrosis virus (ISKNV). The mechanism of action of TC38 against V. vulnificus was explored. The results showed that TC38 killed V. vulnificus cells without lysis of the cell membrane. FITC-labeled TC38 was able to penetrate the cell membrane and bind to DNA and RNA, then disrupt cellular function, eventually leading to cell death. Administration of TC38 to tongue sole significantly improved its defense against V. vulnificus infection. Overall, these results indicate that TC38 is a novel peptide with a broad antimicrobial spectrum. Furthermore, the unique action of TC38 against V. vulnificus adds new insights to the mechanism of action of vertebrate TFPI peptides. Moreover, TC38 is an interesting antimicrobial agent that could be useful in the fight against pathogenic invasion in aquaculture. (C) 2017 Elsevier Ltd. All rights reserved.

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