Heterologous Expression and Antimicrobial Targets of a Novel Glycine-Rich Antimicrobial Peptide from .
Fuente:
PubMed
Guardado en:
| Autores principales: | , , , , , , |
|---|---|
| Formato: | Artículo científico |
| Lenguaje: | en |
| Publicado: |
Marine drugs
2025
|
| Materias: | |
| Acceso en línea: | |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| _version_ | 1868266160097591296 |
|---|---|
| author | Tao, Ming Sun, Aobo Shao, Huishi Ye, Huaiyuan Yu, Guangming Chen, Daigeng Zhang, Wei |
| author_facet | Tao, Ming Sun, Aobo Shao, Huishi Ye, Huaiyuan Yu, Guangming Chen, Daigeng Zhang, Wei Tao, Ming Sun, Aobo Shao, Huishi Ye, Huaiyuan Yu, Guangming Chen, Daigeng Zhang, Wei |
| collection | PubMed - marine biology |
| contents | Heterologous Expression and Antimicrobial Targets of a Novel Glycine-Rich Antimicrobial Peptide from . Tao, Ming Sun, Aobo Shao, Huishi Ye, Huaiyuan Yu, Guangming Chen, Daigeng Zhang, Wei Animals Antimicrobial Peptides Artemia Vibrio alginolyticus Anti-Bacterial Agents Glycine Escherichia coli Molecular Dynamics Simulation Microbial Sensitivity Tests Vibrio Infections Antimicrobial Cationic Peptides Erythrocytes The growing problem of antimicrobial resistance in aquaculture, caused by the excessive and unregulated use of antibiotics, highlights the critical necessity for developing new anti-infective solutions. Based on the characteristics of glycine-rich antimicrobial peptides (AMPs) and transcriptomic data, an antimicrobial peptide, namely Rgly1, was discovered in this study. Subsequently, the peptide was obtained through heterologous expression in , and its antibacterial spectrum was determined. Molecular dynamics simulation and molecular biology experiments were conducted to explore the antibacterial target of Rgly1. Results showed that the mRNA expression level of Rgly1 was significantly upregulated after infection. Rgly1 has broad-spectrum antibacterial activity targeting on bacterial cell membrane, and it may also interact with bacterial DNA. Rgly1 displayed low selectivity for fish red blood cells. These results indicate that Rgly1 is an antimicrobial peptide with considerable potential for application in the development of therapeutic agents. |
| format | Artículo científico |
| id | pubmed_40863648 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Marine drugs |
| record_format | pubmed |
| spellingShingle | Heterologous Expression and Antimicrobial Targets of a Novel Glycine-Rich Antimicrobial Peptide from . Tao, Ming Sun, Aobo Shao, Huishi Ye, Huaiyuan Yu, Guangming Chen, Daigeng Zhang, Wei Animals Antimicrobial Peptides Artemia Vibrio alginolyticus Anti-Bacterial Agents Glycine Escherichia coli Molecular Dynamics Simulation Microbial Sensitivity Tests Vibrio Infections Antimicrobial Cationic Peptides Erythrocytes Heterologous Expression and Antimicrobial Targets of a Novel Glycine-Rich Antimicrobial Peptide from . Tao, Ming Sun, Aobo Shao, Huishi Ye, Huaiyuan Yu, Guangming Chen, Daigeng Zhang, Wei Animals Antimicrobial Peptides Artemia Vibrio alginolyticus Anti-Bacterial Agents Glycine Escherichia coli Molecular Dynamics Simulation Microbial Sensitivity Tests Vibrio Infections Antimicrobial Cationic Peptides Erythrocytes The growing problem of antimicrobial resistance in aquaculture, caused by the excessive and unregulated use of antibiotics, highlights the critical necessity for developing new anti-infective solutions. Based on the characteristics of glycine-rich antimicrobial peptides (AMPs) and transcriptomic data, an antimicrobial peptide, namely Rgly1, was discovered in this study. Subsequently, the peptide was obtained through heterologous expression in , and its antibacterial spectrum was determined. Molecular dynamics simulation and molecular biology experiments were conducted to explore the antibacterial target of Rgly1. Results showed that the mRNA expression level of Rgly1 was significantly upregulated after infection. Rgly1 has broad-spectrum antibacterial activity targeting on bacterial cell membrane, and it may also interact with bacterial DNA. Rgly1 displayed low selectivity for fish red blood cells. These results indicate that Rgly1 is an antimicrobial peptide with considerable potential for application in the development of therapeutic agents. |
| title | Heterologous Expression and Antimicrobial Targets of a Novel Glycine-Rich Antimicrobial Peptide from . |
| topic | Animals Antimicrobial Peptides Artemia Vibrio alginolyticus Anti-Bacterial Agents Glycine Escherichia coli Molecular Dynamics Simulation Microbial Sensitivity Tests Vibrio Infections Antimicrobial Cationic Peptides Erythrocytes |
| url | https://pubmed.ncbi.nlm.nih.gov/40863648/ |