{"title":"氨基酸组成对侧孢菌素类似物抑菌活性的影响。","authors":"Piyush Baindara, Vipul Solanki, Shelley Sardul Singh, Nayudu Nallabelli, Sumeeta Kumari, Pushpanjali Bhardwaj, Vishakha Grover, Krishan Gopal Thakur, Suresh Korpole","doi":"10.1093/jambio/lxaf208","DOIUrl":null,"url":null,"abstract":"<p><strong>Aim: </strong>This study aimed to compare the antimicrobial activity of the structural analogs of a class IId bacteriocin, laterosporulin.</p><p><strong>Methods and results: </strong>The antimicrobial peptide laterosporulin3 (LS3), produced by a Brevibacillus sp. strain SKR3, showed 96% identity to earlier described laterosporulin (LS) and 60% to laterosporulin10 (LS10) in amino acid composition. LS3 has a molecular weight of 5613 Da, the same as LS, yet differs in amino acid composition. Notable differences were found in their antimicrobial activity. Crystal structures of LS3 and LS10 were compared with LS. The analysis revealed that an additional Lys residue in LS3 enhances its net positive charge, leading to increased antimicrobial activity. FITC labeling showed the role of surface-displayed cationic Lys residues in the activity.</p><p><strong>Conclusion: </strong>Crystal structures of three different laterosporulins isolated from various strains of Brevibacillus were compared to understand the structure/function relationship. Results obtained in this study suggest that subtle variations in the amino acid composition of laterosporulins, distribution, and surface accessibility of charged residues can profoundly affect their antimicrobial activity.</p>","PeriodicalId":15036,"journal":{"name":"Journal of Applied Microbiology","volume":" ","pages":""},"PeriodicalIF":3.2000,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The role of amino acid composition in the antibacterial activity of laterosporulin analogs.\",\"authors\":\"Piyush Baindara, Vipul Solanki, Shelley Sardul Singh, Nayudu Nallabelli, Sumeeta Kumari, Pushpanjali Bhardwaj, Vishakha Grover, Krishan Gopal Thakur, Suresh Korpole\",\"doi\":\"10.1093/jambio/lxaf208\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><strong>Aim: </strong>This study aimed to compare the antimicrobial activity of the structural analogs of a class IId bacteriocin, laterosporulin.</p><p><strong>Methods and results: </strong>The antimicrobial peptide laterosporulin3 (LS3), produced by a Brevibacillus sp. strain SKR3, showed 96% identity to earlier described laterosporulin (LS) and 60% to laterosporulin10 (LS10) in amino acid composition. LS3 has a molecular weight of 5613 Da, the same as LS, yet differs in amino acid composition. Notable differences were found in their antimicrobial activity. Crystal structures of LS3 and LS10 were compared with LS. The analysis revealed that an additional Lys residue in LS3 enhances its net positive charge, leading to increased antimicrobial activity. FITC labeling showed the role of surface-displayed cationic Lys residues in the activity.</p><p><strong>Conclusion: </strong>Crystal structures of three different laterosporulins isolated from various strains of Brevibacillus were compared to understand the structure/function relationship. Results obtained in this study suggest that subtle variations in the amino acid composition of laterosporulins, distribution, and surface accessibility of charged residues can profoundly affect their antimicrobial activity.</p>\",\"PeriodicalId\":15036,\"journal\":{\"name\":\"Journal of Applied Microbiology\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":3.2000,\"publicationDate\":\"2025-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Applied Microbiology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1093/jambio/lxaf208\",\"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":"Journal of Applied Microbiology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1093/jambio/lxaf208","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}
The role of amino acid composition in the antibacterial activity of laterosporulin analogs.
Aim: This study aimed to compare the antimicrobial activity of the structural analogs of a class IId bacteriocin, laterosporulin.
Methods and results: The antimicrobial peptide laterosporulin3 (LS3), produced by a Brevibacillus sp. strain SKR3, showed 96% identity to earlier described laterosporulin (LS) and 60% to laterosporulin10 (LS10) in amino acid composition. LS3 has a molecular weight of 5613 Da, the same as LS, yet differs in amino acid composition. Notable differences were found in their antimicrobial activity. Crystal structures of LS3 and LS10 were compared with LS. The analysis revealed that an additional Lys residue in LS3 enhances its net positive charge, leading to increased antimicrobial activity. FITC labeling showed the role of surface-displayed cationic Lys residues in the activity.
Conclusion: Crystal structures of three different laterosporulins isolated from various strains of Brevibacillus were compared to understand the structure/function relationship. Results obtained in this study suggest that subtle variations in the amino acid composition of laterosporulins, distribution, and surface accessibility of charged residues can profoundly affect their antimicrobial activity.
期刊介绍：
Journal of & Letters in Applied Microbiology are two of the flagship research journals of the Society for Applied Microbiology (SfAM). For more than 75 years they have been publishing top quality research and reviews in the broad field of applied microbiology. The journals are provided to all SfAM members as well as having a global online readership totalling more than 500,000 downloads per year in more than 200 countries. Submitting authors can expect fast decision and publication times, averaging 33 days to first decision and 34 days from acceptance to online publication. There are no page charges.
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