{"title":"蜡样芽孢杆菌抗铜绿假单胞菌n -酰基高丝氨酸内酯酶和青霉素酰化酶II:伽马辐射对其群体猝灭活性影响的计算机和体外研究","authors":"Radwa N. Morgan, Reham R. El-Behery","doi":"10.1016/j.enzmictec.2025.110699","DOIUrl":null,"url":null,"abstract":"<div><div>This study explored the quorum quenching (QQ) activities of ISM25 strain, sourced from an environmental setting, on pathogenic <em>Pseudomonas aeruginosa</em> isolates. The isolate ISM25 was first screened for the presence of both <em>AiiA</em> acyl homoserine lactonase and penicillin <em>acylase II</em> genes. The in silico investigation focused on examining the physiochemical properties and QQ activities in relation to both short (<C8) and long chain (>C12) homoserine lactones (HSLs) utilizing AutoDock Vina docking tests. Potential interactions between the acylase II enzyme and carbapenem antibiotics were also investigated during the in silico docking tests. Afterwards, the in vitro QQ activity of ISM25 crude protein extract was assessed against the biofilm index, AHLs molecules, and meropenem minimum inhibitory concentrations of pathogenic <em>P. aeruginosa</em> isolates. The findings from the in silico docking analysis were supported by the crude protein extract's capacity to hydrolyze AHLs generated by the pathogenic <em>P. aeruginosa</em> isolate, as well as the reference C12-HSL signal molecule. The notable decrease in biofilm indices (P < 0.05) following exposure to the crude ISM25 extract further corroborated the expression of both QQ enzymes by the ISM25 isolate and their in silico QQ activity. The crude extract from ISM25 lowered the MIC and sensitized <em>P. aeruginosa</em> to meropenem (P < 0.05), suggesting that ISM25 crude extract containing acylase II can be administered in conjunction with meropenem without affecting its efficacy. Finally, exposure of ISM25 to gamma radiation did not impair its QQ activity at doses below 100 Gy, however, QQ activity was nearly abolished at radiation dose ≥ 500 Gy.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110699"},"PeriodicalIF":3.7000,"publicationDate":"2025-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Bacillus cereus N-acyl homoserine lactonase and penicillin acylase II against Pseudomonas aeruginosa: An In silico and In vitro investigations exploring the effects of gamma radiation on their quorum quenching activity\",\"authors\":\"Radwa N. Morgan, Reham R. El-Behery\",\"doi\":\"10.1016/j.enzmictec.2025.110699\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>This study explored the quorum quenching (QQ) activities of ISM25 strain, sourced from an environmental setting, on pathogenic <em>Pseudomonas aeruginosa</em> isolates. The isolate ISM25 was first screened for the presence of both <em>AiiA</em> acyl homoserine lactonase and penicillin <em>acylase II</em> genes. The in silico investigation focused on examining the physiochemical properties and QQ activities in relation to both short (<C8) and long chain (>C12) homoserine lactones (HSLs) utilizing AutoDock Vina docking tests. Potential interactions between the acylase II enzyme and carbapenem antibiotics were also investigated during the in silico docking tests. Afterwards, the in vitro QQ activity of ISM25 crude protein extract was assessed against the biofilm index, AHLs molecules, and meropenem minimum inhibitory concentrations of pathogenic <em>P. aeruginosa</em> isolates. The findings from the in silico docking analysis were supported by the crude protein extract's capacity to hydrolyze AHLs generated by the pathogenic <em>P. aeruginosa</em> isolate, as well as the reference C12-HSL signal molecule. The notable decrease in biofilm indices (P < 0.05) following exposure to the crude ISM25 extract further corroborated the expression of both QQ enzymes by the ISM25 isolate and their in silico QQ activity. The crude extract from ISM25 lowered the MIC and sensitized <em>P. aeruginosa</em> to meropenem (P < 0.05), suggesting that ISM25 crude extract containing acylase II can be administered in conjunction with meropenem without affecting its efficacy. Finally, exposure of ISM25 to gamma radiation did not impair its QQ activity at doses below 100 Gy, however, QQ activity was nearly abolished at radiation dose ≥ 500 Gy.</div></div>\",\"PeriodicalId\":11770,\"journal\":{\"name\":\"Enzyme and Microbial Technology\",\"volume\":\"190 \",\"pages\":\"Article 110699\"},\"PeriodicalIF\":3.7000,\"publicationDate\":\"2025-06-21\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Enzyme and Microbial Technology\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S014102292500119X\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOTECHNOLOGY & APPLIED MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Enzyme and Microbial Technology","FirstCategoryId":"5","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S014102292500119X","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
Bacillus cereus N-acyl homoserine lactonase and penicillin acylase II against Pseudomonas aeruginosa: An In silico and In vitro investigations exploring the effects of gamma radiation on their quorum quenching activity
This study explored the quorum quenching (QQ) activities of ISM25 strain, sourced from an environmental setting, on pathogenic Pseudomonas aeruginosa isolates. The isolate ISM25 was first screened for the presence of both AiiA acyl homoserine lactonase and penicillin acylase II genes. The in silico investigation focused on examining the physiochemical properties and QQ activities in relation to both short (<C8) and long chain (>C12) homoserine lactones (HSLs) utilizing AutoDock Vina docking tests. Potential interactions between the acylase II enzyme and carbapenem antibiotics were also investigated during the in silico docking tests. Afterwards, the in vitro QQ activity of ISM25 crude protein extract was assessed against the biofilm index, AHLs molecules, and meropenem minimum inhibitory concentrations of pathogenic P. aeruginosa isolates. The findings from the in silico docking analysis were supported by the crude protein extract's capacity to hydrolyze AHLs generated by the pathogenic P. aeruginosa isolate, as well as the reference C12-HSL signal molecule. The notable decrease in biofilm indices (P < 0.05) following exposure to the crude ISM25 extract further corroborated the expression of both QQ enzymes by the ISM25 isolate and their in silico QQ activity. The crude extract from ISM25 lowered the MIC and sensitized P. aeruginosa to meropenem (P < 0.05), suggesting that ISM25 crude extract containing acylase II can be administered in conjunction with meropenem without affecting its efficacy. Finally, exposure of ISM25 to gamma radiation did not impair its QQ activity at doses below 100 Gy, however, QQ activity was nearly abolished at radiation dose ≥ 500 Gy.
期刊介绍:
Enzyme and Microbial Technology is an international, peer-reviewed journal publishing original research and reviews, of biotechnological significance and novelty, on basic and applied aspects of the science and technology of processes involving the use of enzymes, micro-organisms, animal cells and plant cells.
We especially encourage submissions on:
Biocatalysis and the use of Directed Evolution in Synthetic Biology and Biotechnology
Biotechnological Production of New Bioactive Molecules, Biomaterials, Biopharmaceuticals, and Biofuels
New Imaging Techniques and Biosensors, especially as applicable to Healthcare and Systems Biology
New Biotechnological Approaches in Genomics, Proteomics and Metabolomics
Metabolic Engineering, Biomolecular Engineering and Nanobiotechnology
Manuscripts which report isolation, purification, immobilization or utilization of organisms or enzymes which are already well-described in the literature are not suitable for publication in EMT, unless their primary purpose is to report significant new findings or approaches which are of broad biotechnological importance. Similarly, manuscripts which report optimization studies on well-established processes are inappropriate. EMT does not accept papers dealing with mathematical modeling unless they report significant, new experimental data.