Antimicrobial Mechanism of Antimicrobial Peptide LL-1 against Salmonella
To explore the antibacterial effect and mechanism of antimicrobial peptide LL-1 against Salmonella, the minimum inhibitory concentration (MIC) was determined by the doubling dilution method, and the antibacterial effect was evaluated by the growth inhibition curve. Then, the bacterial morphology was...
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China Food Publishing Company
2025-02-01
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| Series: | Shipin Kexue |
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| Online Access: | https://www.spkx.net.cn/fileup/1002-6630/PDF/2025-46-4-012.pdf |
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| author | WANG Yuhang, ZHOU Lingling, ZHOU Yaoling, SA Junmeng, ZHANG Yuanchen, MA Zengjun, LIAN Kaiqi |
| author_facet | WANG Yuhang, ZHOU Lingling, ZHOU Yaoling, SA Junmeng, ZHANG Yuanchen, MA Zengjun, LIAN Kaiqi |
| author_sort | WANG Yuhang, ZHOU Lingling, ZHOU Yaoling, SA Junmeng, ZHANG Yuanchen, MA Zengjun, LIAN Kaiqi |
| collection | DOAJ |
| description | To explore the antibacterial effect and mechanism of antimicrobial peptide LL-1 against Salmonella, the minimum inhibitory concentration (MIC) was determined by the doubling dilution method, and the antibacterial effect was evaluated by the growth inhibition curve. Then, the bacterial morphology was observed using scanning electron microscopy (SEM) and transmission electron microscopy (TEM). The effect of LL-1 on the cell wall and cell membrane of Salmonella was evaluated by detecting the leakage of intracellular nucleic acids, proteins and alkaline phosphatase (ALP) as well as by conducting propidium iodide (PI) staining experiments. The binding of LL-1 to Salmonella DNA was detected by nucleic acid gel electrophoresis. Finally, the effect of LL-1 on the energy metabolism of Salmonella was evaluated by measuring the activities of intracellular succinate dehydrogenase (SDH), NADP-malate dehydrogenase (NADP-MDH) and ATP levels. The results showed that the MIC was 6.25 μg/mL, and LL-1 had a good antibacterial effect in dose- and time-dependent manners. Salmonella treated with LL-1 showed morphological changes such as cell shrinkage, cell membrane dissolution, and plasmolysis. LL-1 resulted in the leakage of intracellular nucleic acids, proteins and ALP and an increase in the fluorescence intensity of PI-stained bacterial cells. Additionally, LL-1 could bind to bacterial DNA. Increasing LL-1 concentration resulted in a decrease in the intracellular ATP content, SDH and NADP-MDH activities. In conclusion, LL-1 could exert its antibacterial activity against Salmonella by increasing the permeability of the cell membrane and cell wall, thereby causing the leakage of intracellular contents, binding to DNA, and affecting bacterial energy metabolism. This study lays the foundation for further research on the antibacterial mechanism and application of LL-1. |
| format | Article |
| id | doaj-art-e4b8cfb49e82407e817001ecc101812a |
| institution | DOAJ |
| issn | 1002-6630 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | China Food Publishing Company |
| record_format | Article |
| series | Shipin Kexue |
| spelling | doaj-art-e4b8cfb49e82407e817001ecc101812a2025-08-20T03:11:54ZengChina Food Publishing CompanyShipin Kexue1002-66302025-02-0146411011610.7506/spkx1002-6630-20240602-002Antimicrobial Mechanism of Antimicrobial Peptide LL-1 against SalmonellaWANG Yuhang, ZHOU Lingling, ZHOU Yaoling, SA Junmeng, ZHANG Yuanchen, MA Zengjun, LIAN Kaiqi0(1. School of Biology and Food Engineering, Anyang Institute of Technology, Anyang 455000, China; 2. College of Animal Science and Technology, Hebei Normal University of Science and Technology, Qinhuangdao 066004, China; 3. Henan Joint International Research Laboratory of Veterinary Biologics Research and Application, Anyang 455000, China; 4. Taihang Mountain Forest Pests Observation and Research Station of Henan Province, Linzhou 456550, China)To explore the antibacterial effect and mechanism of antimicrobial peptide LL-1 against Salmonella, the minimum inhibitory concentration (MIC) was determined by the doubling dilution method, and the antibacterial effect was evaluated by the growth inhibition curve. Then, the bacterial morphology was observed using scanning electron microscopy (SEM) and transmission electron microscopy (TEM). The effect of LL-1 on the cell wall and cell membrane of Salmonella was evaluated by detecting the leakage of intracellular nucleic acids, proteins and alkaline phosphatase (ALP) as well as by conducting propidium iodide (PI) staining experiments. The binding of LL-1 to Salmonella DNA was detected by nucleic acid gel electrophoresis. Finally, the effect of LL-1 on the energy metabolism of Salmonella was evaluated by measuring the activities of intracellular succinate dehydrogenase (SDH), NADP-malate dehydrogenase (NADP-MDH) and ATP levels. The results showed that the MIC was 6.25 μg/mL, and LL-1 had a good antibacterial effect in dose- and time-dependent manners. Salmonella treated with LL-1 showed morphological changes such as cell shrinkage, cell membrane dissolution, and plasmolysis. LL-1 resulted in the leakage of intracellular nucleic acids, proteins and ALP and an increase in the fluorescence intensity of PI-stained bacterial cells. Additionally, LL-1 could bind to bacterial DNA. Increasing LL-1 concentration resulted in a decrease in the intracellular ATP content, SDH and NADP-MDH activities. In conclusion, LL-1 could exert its antibacterial activity against Salmonella by increasing the permeability of the cell membrane and cell wall, thereby causing the leakage of intracellular contents, binding to DNA, and affecting bacterial energy metabolism. This study lays the foundation for further research on the antibacterial mechanism and application of LL-1.https://www.spkx.net.cn/fileup/1002-6630/PDF/2025-46-4-012.pdfsalmonella; antimicrobial peptides; antimicrobial mechanism; foodborne pathogens; cell membrane; energy metabolism |
| spellingShingle | WANG Yuhang, ZHOU Lingling, ZHOU Yaoling, SA Junmeng, ZHANG Yuanchen, MA Zengjun, LIAN Kaiqi Antimicrobial Mechanism of Antimicrobial Peptide LL-1 against Salmonella Shipin Kexue salmonella; antimicrobial peptides; antimicrobial mechanism; foodborne pathogens; cell membrane; energy metabolism |
| title | Antimicrobial Mechanism of Antimicrobial Peptide LL-1 against Salmonella |
| title_full | Antimicrobial Mechanism of Antimicrobial Peptide LL-1 against Salmonella |
| title_fullStr | Antimicrobial Mechanism of Antimicrobial Peptide LL-1 against Salmonella |
| title_full_unstemmed | Antimicrobial Mechanism of Antimicrobial Peptide LL-1 against Salmonella |
| title_short | Antimicrobial Mechanism of Antimicrobial Peptide LL-1 against Salmonella |
| title_sort | antimicrobial mechanism of antimicrobial peptide ll 1 against salmonella |
| topic | salmonella; antimicrobial peptides; antimicrobial mechanism; foodborne pathogens; cell membrane; energy metabolism |
| url | https://www.spkx.net.cn/fileup/1002-6630/PDF/2025-46-4-012.pdf |
| work_keys_str_mv | AT wangyuhangzhoulinglingzhouyaolingsajunmengzhangyuanchenmazengjunliankaiqi antimicrobialmechanismofantimicrobialpeptidell1againstsalmonella |