Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (<i>Trachinotus ovatus</i>)
Hepcidin, a cysteine-rich antimicrobial peptide, has a highly conserved gene structure in teleosts, and it plays an essential role in host immune response against various pathogenic bacteria. Nonetheless, few studies on the antibacterial mechanism of hepcidin in golden pompano (<i>Trachinotus...
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MDPI AG
2023-05-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/11/9251 |
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| author | Zhengshi Zhang Yongcan Zhou Han Zhang Xiangyu Du Zhenjie Cao Ying Wu Chunsheng Liu Yun Sun |
| author_facet | Zhengshi Zhang Yongcan Zhou Han Zhang Xiangyu Du Zhenjie Cao Ying Wu Chunsheng Liu Yun Sun |
| author_sort | Zhengshi Zhang |
| collection | DOAJ |
| description | Hepcidin, a cysteine-rich antimicrobial peptide, has a highly conserved gene structure in teleosts, and it plays an essential role in host immune response against various pathogenic bacteria. Nonetheless, few studies on the antibacterial mechanism of hepcidin in golden pompano (<i>Trachinotus ovatus</i>) have been reported. In this study, we synthesized a derived peptide, TroHepc2-22, from the mature peptide of <i>T. ovatus</i> hepcidin2. Our results showed that TroHepc2-22 has superior antibacterial abilities against both Gram-negative (<i>Vibrio harveyi</i> and <i>Edwardsiella piscicida</i>) and Gram-positive (<i>Staphylococcus aureus</i> and <i>Streptococcus agalactiae</i>) bacteria. Based on the results of a bacterial membrane depolarization assay and propidium iodide (PI) staining assay in vitro, TroHepc2-22 displayed antimicrobial activity by inducing the bacterial membrane depolarization and changing the bacterial membrane permeability. Scanning electron microscopy (SEM) visualization illustrated that TroHepc2-22 brought about membrane rupturing and the leakage of the cytoplasm for the bacteria. In addition, TroHepc2-22 was verified to have hydrolytic activity on bacterial genomic DNA in view of the results of the gel retardation assay. In terms of the in vivo assay, the bacterial loads of <i>V. harveyi</i> in the tested immune tissues (liver, spleen, and head kidney) were significantly reduced in <i>T. ovatus</i>, revealing that TroHepc2-22 significantly enhanced the resistance against <i>V. harveyi</i> infection. Furthermore, the expressions of immune-related genes, including tumor necrosis factor-α (<i>TNF-α</i>), interferon-γ (<i>IFN-γ</i>), interleukin 1-β (<i>IL-1β</i>), <i>IL-6</i>, Toll-like receptor 1 (<i>TLR1</i>), and myeloid differentiation factor 88 (<i>MyD88</i>) were significantly increased, indicating that TroHepc2-22 might regulate inflammatory cytokines and activate immune-related signaling pathways. To summarize, TroHepc2-22 possesses appreciable antimicrobial activity and plays a vital role in resisting bacterial infection. The observation of our present study unveils the excellent application prospect of hepcidin as a substitute for antibiotics to resist pathogenic microorganisms in teleosts. |
| first_indexed | 2024-03-11T03:06:39Z |
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| language | English |
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| spelling | doaj.art-753d5ede199b4ffd85e57dde4212a5082023-11-18T07:56:27ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-05-012411925110.3390/ijms24119251Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (<i>Trachinotus ovatus</i>)Zhengshi Zhang0Yongcan Zhou1Han Zhang2Xiangyu Du3Zhenjie Cao4Ying Wu5Chunsheng Liu6Yun Sun7Sanya Nanfan Research Institute, Hainan University, Sanya 572022, ChinaSanya Nanfan Research Institute, Hainan University, Sanya 572022, ChinaSanya Nanfan Research Institute, Hainan University, Sanya 572022, ChinaSanya Nanfan Research Institute, Hainan University, Sanya 572022, ChinaSanya Nanfan Research Institute, Hainan University, Sanya 572022, ChinaSanya Nanfan Research Institute, Hainan University, Sanya 572022, ChinaSanya Nanfan Research Institute, Hainan University, Sanya 572022, ChinaSanya Nanfan Research Institute, Hainan University, Sanya 572022, ChinaHepcidin, a cysteine-rich antimicrobial peptide, has a highly conserved gene structure in teleosts, and it plays an essential role in host immune response against various pathogenic bacteria. Nonetheless, few studies on the antibacterial mechanism of hepcidin in golden pompano (<i>Trachinotus ovatus</i>) have been reported. In this study, we synthesized a derived peptide, TroHepc2-22, from the mature peptide of <i>T. ovatus</i> hepcidin2. Our results showed that TroHepc2-22 has superior antibacterial abilities against both Gram-negative (<i>Vibrio harveyi</i> and <i>Edwardsiella piscicida</i>) and Gram-positive (<i>Staphylococcus aureus</i> and <i>Streptococcus agalactiae</i>) bacteria. Based on the results of a bacterial membrane depolarization assay and propidium iodide (PI) staining assay in vitro, TroHepc2-22 displayed antimicrobial activity by inducing the bacterial membrane depolarization and changing the bacterial membrane permeability. Scanning electron microscopy (SEM) visualization illustrated that TroHepc2-22 brought about membrane rupturing and the leakage of the cytoplasm for the bacteria. In addition, TroHepc2-22 was verified to have hydrolytic activity on bacterial genomic DNA in view of the results of the gel retardation assay. In terms of the in vivo assay, the bacterial loads of <i>V. harveyi</i> in the tested immune tissues (liver, spleen, and head kidney) were significantly reduced in <i>T. ovatus</i>, revealing that TroHepc2-22 significantly enhanced the resistance against <i>V. harveyi</i> infection. Furthermore, the expressions of immune-related genes, including tumor necrosis factor-α (<i>TNF-α</i>), interferon-γ (<i>IFN-γ</i>), interleukin 1-β (<i>IL-1β</i>), <i>IL-6</i>, Toll-like receptor 1 (<i>TLR1</i>), and myeloid differentiation factor 88 (<i>MyD88</i>) were significantly increased, indicating that TroHepc2-22 might regulate inflammatory cytokines and activate immune-related signaling pathways. To summarize, TroHepc2-22 possesses appreciable antimicrobial activity and plays a vital role in resisting bacterial infection. The observation of our present study unveils the excellent application prospect of hepcidin as a substitute for antibiotics to resist pathogenic microorganisms in teleosts.https://www.mdpi.com/1422-0067/24/11/9251<i>Trachinotus ovatus</i>hepcidinantimicrobial peptideTroHepc2-22antibacterial mechanisms |
| spellingShingle | Zhengshi Zhang Yongcan Zhou Han Zhang Xiangyu Du Zhenjie Cao Ying Wu Chunsheng Liu Yun Sun Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (<i>Trachinotus ovatus</i>) International Journal of Molecular Sciences <i>Trachinotus ovatus</i> hepcidin antimicrobial peptide TroHepc2-22 antibacterial mechanisms |
| title | Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (<i>Trachinotus ovatus</i>) |
| title_full | Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (<i>Trachinotus ovatus</i>) |
| title_fullStr | Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (<i>Trachinotus ovatus</i>) |
| title_full_unstemmed | Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (<i>Trachinotus ovatus</i>) |
| title_short | Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (<i>Trachinotus ovatus</i>) |
| title_sort | antibacterial activity and mechanisms of trohepc2 22 a derived peptide of hepcidin2 from golden pompano i trachinotus ovatus i |
| topic | <i>Trachinotus ovatus</i> hepcidin antimicrobial peptide TroHepc2-22 antibacterial mechanisms |
| url | https://www.mdpi.com/1422-0067/24/11/9251 |
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