Antimicrobial peptide mSshep 1 from Sebastes schlegelii combines broad-spectrum antibacterial activity, membrane-disruptive mechanism and in vivo protective efficacy.
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| Format: | Artículo científico |
| Language: | en |
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Fish & shellfish immunology
2026
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| author | Jing, Hao Wang, Guang-Hua Yang, Kai Chen, Zi-Yue Zhu, Zhi-Shu Sun, Nuo Du, Yi-Lin Wang, Zi-Qi Zhang, Min |
| author_facet | Jing, Hao Wang, Guang-Hua Yang, Kai Chen, Zi-Yue Zhu, Zhi-Shu Sun, Nuo Du, Yi-Lin Wang, Zi-Qi Zhang, Min Jing, Hao Wang, Guang-Hua Yang, Kai Chen, Zi-Yue Zhu, Zhi-Shu Sun, Nuo Du, Yi-Lin Wang, Zi-Qi Zhang, Min |
| collection | PubMed - marine biology |
| contents | Antimicrobial peptide mSshep 1 from Sebastes schlegelii combines broad-spectrum antibacterial activity, membrane-disruptive mechanism and in vivo protective efficacy. Jing, Hao Wang, Guang-Hua Yang, Kai Chen, Zi-Yue Zhu, Zhi-Shu Sun, Nuo Du, Yi-Lin Wang, Zi-Qi Zhang, Min Animals Fish Proteins Fish Diseases Hepcidins Anti-Bacterial Agents Immunity, Innate Antimicrobial Peptides Gram-Negative Bacterial Infections Aeromonas hydrophila Fishes Hepcidins, a family of cysteine-rich antimicrobial peptides, play a pivotal role in the innate immune defense of teleosts. This study aimed to characterize the antibacterial activity, mechanism of action, and in vitro/in vivo protective efficacy of the mature peptide mSshep 1 derived from hepcidin 1 of Sebastes schlegelii (Sshepcidin 1), and to verify the functional role of Sshepcidin 1 via RNA interference (RNAi). Time-kill kinetic assay showed that mSshep 1 exhibited rapid and broad-spectrum bactericidal activity against Staphylococcus aureus, Edwardsiella piscicida, Listonella anguillarum, and Aeromonas hydrophila, with complete eradication of all tested strains within 120 min. Thermal stability analysis revealed that mSshep 1 retained significant antibacterial activity against most pathogens even after treatment at 100 °C for 30 min, and circular dichroism spectroscopy confirmed only minor conformational changes without substantial secondary structure alterations. Mechanistically, mSshep 1 exerted bactericidal effects by disrupting bacterial membrane integrity, as evidenced by increased propidium iodide penetration, elevated intracellular reactive oxygen species levels, and obvious morphological damage observed via scanning and transmission electron microscopy. In vitro, mSshep 1 showed no cytotoxicity to HEK293T, EPC, and SSI cells at concentrations up to 128 μM, and effectively eliminated intracellular E. piscicida in SSI cells while upregulating the expression of immune-related genes. In vivo experiments demonstrated that pre-injection of mSshep 1 (1, 2, 5 μg/g body weight) significantly improved the survival rate of S. schlegelii challenged with E. piscicida and reduced bacterial loads in the liver, spleen, and head kidney. RNAi analysis showed that si-Sshep1-1 (2 μg/g body weight) stably silenced Sshepcidin 1 expression in multiple tissues, and Sshepcidin 1 knockdown significantly increased bacterial loads in E. piscicida-challenged fish and disrupted the expression balance of immune-related genes. Collectively, these findings confirm that mSshep 1 is a promising candidate for the development of novel antibacterial agents in aquaculture, and Sshepcidin 1 plays a crucial role in the innate immune defense of S. schlegelii against bacterial infections. |
| format | Artículo científico |
| id | pubmed_41651046 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Fish & shellfish immunology |
| record_format | pubmed |
| spellingShingle | Antimicrobial peptide mSshep 1 from Sebastes schlegelii combines broad-spectrum antibacterial activity, membrane-disruptive mechanism and in vivo protective efficacy. Jing, Hao Wang, Guang-Hua Yang, Kai Chen, Zi-Yue Zhu, Zhi-Shu Sun, Nuo Du, Yi-Lin Wang, Zi-Qi Zhang, Min Animals Fish Proteins Fish Diseases Hepcidins Anti-Bacterial Agents Immunity, Innate Antimicrobial Peptides Gram-Negative Bacterial Infections Aeromonas hydrophila Fishes Antimicrobial peptide mSshep 1 from Sebastes schlegelii combines broad-spectrum antibacterial activity, membrane-disruptive mechanism and in vivo protective efficacy. Jing, Hao Wang, Guang-Hua Yang, Kai Chen, Zi-Yue Zhu, Zhi-Shu Sun, Nuo Du, Yi-Lin Wang, Zi-Qi Zhang, Min Animals Fish Proteins Fish Diseases Hepcidins Anti-Bacterial Agents Immunity, Innate Antimicrobial Peptides Gram-Negative Bacterial Infections Aeromonas hydrophila Fishes Hepcidins, a family of cysteine-rich antimicrobial peptides, play a pivotal role in the innate immune defense of teleosts. This study aimed to characterize the antibacterial activity, mechanism of action, and in vitro/in vivo protective efficacy of the mature peptide mSshep 1 derived from hepcidin 1 of Sebastes schlegelii (Sshepcidin 1), and to verify the functional role of Sshepcidin 1 via RNA interference (RNAi). Time-kill kinetic assay showed that mSshep 1 exhibited rapid and broad-spectrum bactericidal activity against Staphylococcus aureus, Edwardsiella piscicida, Listonella anguillarum, and Aeromonas hydrophila, with complete eradication of all tested strains within 120 min. Thermal stability analysis revealed that mSshep 1 retained significant antibacterial activity against most pathogens even after treatment at 100 °C for 30 min, and circular dichroism spectroscopy confirmed only minor conformational changes without substantial secondary structure alterations. Mechanistically, mSshep 1 exerted bactericidal effects by disrupting bacterial membrane integrity, as evidenced by increased propidium iodide penetration, elevated intracellular reactive oxygen species levels, and obvious morphological damage observed via scanning and transmission electron microscopy. In vitro, mSshep 1 showed no cytotoxicity to HEK293T, EPC, and SSI cells at concentrations up to 128 μM, and effectively eliminated intracellular E. piscicida in SSI cells while upregulating the expression of immune-related genes. In vivo experiments demonstrated that pre-injection of mSshep 1 (1, 2, 5 μg/g body weight) significantly improved the survival rate of S. schlegelii challenged with E. piscicida and reduced bacterial loads in the liver, spleen, and head kidney. RNAi analysis showed that si-Sshep1-1 (2 μg/g body weight) stably silenced Sshepcidin 1 expression in multiple tissues, and Sshepcidin 1 knockdown significantly increased bacterial loads in E. piscicida-challenged fish and disrupted the expression balance of immune-related genes. Collectively, these findings confirm that mSshep 1 is a promising candidate for the development of novel antibacterial agents in aquaculture, and Sshepcidin 1 plays a crucial role in the innate immune defense of S. schlegelii against bacterial infections. |
| title | Antimicrobial peptide mSshep 1 from Sebastes schlegelii combines broad-spectrum antibacterial activity, membrane-disruptive mechanism and in vivo protective efficacy. |
| topic | Animals Fish Proteins Fish Diseases Hepcidins Anti-Bacterial Agents Immunity, Innate Antimicrobial Peptides Gram-Negative Bacterial Infections Aeromonas hydrophila Fishes |
| url | https://pubmed.ncbi.nlm.nih.gov/41651046/ |