TC38, a teleost TFPI‐2 peptide that kills bacteria via penetration of the cell membrane and interaction with nucleic acids
TC38, a teleost TFPI‐2 peptide that kills bacteria via penetration of the cell membrane and interaction with nucleic acids
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DOI：
10.1016/j.fsi.2017.03.001
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发表时间：
2017-05
影响因子：
4.7
通讯作者：
M. Zhang;B. Yue;Ailing Zhang;Guang-hua Wang;Y. Liu;Shun Zhou;Shun-Feng Cheng;Ningqiu Li
中科院分区：
文献类型：
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作者：
M. Zhang;B. Yue;Ailing Zhang;Guang-hua Wang;Y. Liu;Shun Zhou;Shun-Feng Cheng;Ningqiu Li
组织因子途径抑制剂2 （TFPI-2）是TFPI-1的类似物，是一种有效的内源性组织因子（TF）介导的凝血抑制剂。最近的报道已经证明，人类和其他几种脊椎动物的TFPI-2肽的c端对革兰氏阳性和革兰氏阴性细菌具有抗菌活性。在我们之前的研究中，我们报道了舌底（Cynoglossus semilaevis）中TFPI-2肽TC38对黄体微球菌有活性。在本研究中，我们进一步研究了TC38在舌底中的抗菌谱、作用机制和功能。结果表明，TC38对革兰氏阴性菌鱼肠弧菌、litoralis弧菌、副溶血性弧菌、创伤弧菌以及鱼巨细胞病毒、感染性脾肾坏死病毒（ISKNV）均有活性。TC38抗v的作用机理。vulnificuswas探索。结果表明，TC38对病毒有杀伤作用。无细胞膜溶解的创伤细胞。fitc标记的TC38能够穿透细胞膜，与DNA和RNA结合，破坏细胞功能，最终导致细胞死亡。舌底注射TC38后，其抗病毒能力明显增强。vulnificusinfection。总之，这些结果表明TC38是一种具有广泛抗菌谱的新型肽。此外，TC38对v的独特作用。创伤为脊椎动物TFPI肽的作用机制提供了新的见解。此外，TC38是一种有趣的抗菌剂，可用于对抗水产养殖中的病原入侵。
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 againstMicrococcus 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 bacteriaVibrio ichthyoenteri,Vibrio litoralis,Vibrio parahaemolyticus, andVibrio vulnificus, as well as the fishMegalocytivirus, infectious spleen and kidney necrosis virus (ISKNV). The mechanism of action of TC38 againstV. vulnificuswas explored. The results showed that TC38 killedV. vulnificuscells 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 againstV. vulnificusinfection. Overall, these results indicate that TC38 is a novel peptide with a broad antimicrobial spectrum. Furthermore, the unique action of TC38 againstV. vulnificusadds 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.