{"title":"地衣芽孢杆菌胞外蛋白的 LC-MS/MS 图谱分析及对白色念珠菌抗真菌潜力的分析","authors":"Jyoti Sankar Prusty, Awanish Kumar","doi":"10.1016/j.jprot.2024.105228","DOIUrl":null,"url":null,"abstract":"<div><p><em>Candida albicans</em>, a significant human pathogenic fungus, employs hydrolytic proteases for host invasion. Conventional antifungal agents are reported with resistance issues from around the world. This study investigates the role of <em>Bacillus licheniformis</em> extracellular proteins (ECP) as effective antifungal peptides (AFPs). The aim was to identify and characterize the ECP of <em>B. licheniformis</em> through LC-MS/MS and bioinformatics analysis. LC-MS/MS analysis identified 326 proteins with 69 putative ECP, further analyzed <em>in silico</em>. Of these, 21 peptides exhibited antifungal properties revealed by classAMP tool and are predominantly anionic. Peptide-protein docking revealed interactions between AFPs like Peptide chain release factor 1 (Q65DV1_Seq1: SASEQLSDAK) and Putative carboxy peptidase (Q65IF0_Seq7: SDSSLEDQDFILESK) with <em>C. albicans</em> virulent SAP5 proteins (PDB ID <span>2QZX</span><svg><path></path></svg>), forming hydrogen bonds and significant Pi-Pi interactions. The identification of <em>B. licheniformis</em> ECP is the novelty of the study that sheds light on their antifungal potential. The identified AFPs, particularly those interacting with bonafide pharmaceutical targets SAP5 of <em>C. albicans</em> represent promising avenues for the development of antifungal treatments with AFPs that could be the pursuit of a novel therapeutic strategy against <em>C. albicans</em>.</p></div><div><h3>Significance of study</h3><p>The purpose of this work was to carry out proteomic profiling of the secretome of <em>B. licheniformis</em>. Previously, the efficacy of <em>Bacillus licheniformis</em> extracellular proteins against <em>Candida albicans</em> was investigated and documented in a recently communicated manuscript, showcasing the antifungal activity of these proteins. In order to achieve high-throughput identification of ES (Excretory-secretory) proteins, the utilization of liquid chromatography tandem mass spectrometry (LC-MS) was utilized. There was a lack of comprehensive research on AFPs in <em>B. licheniformis</em>, nevertheless. The proteins secreted by <em>B. licheniformis</em> in liquid medium were initially discovered using liquid chromatography-tandem mass spectrometry (LC-MS) analysis and identification in order to immediately characterize the unidentified active metabolites in fermentation broth.</p></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"303 ","pages":"Article 105228"},"PeriodicalIF":2.8000,"publicationDate":"2024-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"LC-MS/MS profiling and analysis of Bacillus licheniformis extracellular proteins for antifungal potential against Candida albicans\",\"authors\":\"Jyoti Sankar Prusty, Awanish Kumar\",\"doi\":\"10.1016/j.jprot.2024.105228\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><em>Candida albicans</em>, a significant human pathogenic fungus, employs hydrolytic proteases for host invasion. Conventional antifungal agents are reported with resistance issues from around the world. This study investigates the role of <em>Bacillus licheniformis</em> extracellular proteins (ECP) as effective antifungal peptides (AFPs). The aim was to identify and characterize the ECP of <em>B. licheniformis</em> through LC-MS/MS and bioinformatics analysis. LC-MS/MS analysis identified 326 proteins with 69 putative ECP, further analyzed <em>in silico</em>. Of these, 21 peptides exhibited antifungal properties revealed by classAMP tool and are predominantly anionic. Peptide-protein docking revealed interactions between AFPs like Peptide chain release factor 1 (Q65DV1_Seq1: SASEQLSDAK) and Putative carboxy peptidase (Q65IF0_Seq7: SDSSLEDQDFILESK) with <em>C. albicans</em> virulent SAP5 proteins (PDB ID <span>2QZX</span><svg><path></path></svg>), forming hydrogen bonds and significant Pi-Pi interactions. The identification of <em>B. licheniformis</em> ECP is the novelty of the study that sheds light on their antifungal potential. The identified AFPs, particularly those interacting with bonafide pharmaceutical targets SAP5 of <em>C. albicans</em> represent promising avenues for the development of antifungal treatments with AFPs that could be the pursuit of a novel therapeutic strategy against <em>C. albicans</em>.</p></div><div><h3>Significance of study</h3><p>The purpose of this work was to carry out proteomic profiling of the secretome of <em>B. licheniformis</em>. Previously, the efficacy of <em>Bacillus licheniformis</em> extracellular proteins against <em>Candida albicans</em> was investigated and documented in a recently communicated manuscript, showcasing the antifungal activity of these proteins. In order to achieve high-throughput identification of ES (Excretory-secretory) proteins, the utilization of liquid chromatography tandem mass spectrometry (LC-MS) was utilized. There was a lack of comprehensive research on AFPs in <em>B. licheniformis</em>, nevertheless. The proteins secreted by <em>B. licheniformis</em> in liquid medium were initially discovered using liquid chromatography-tandem mass spectrometry (LC-MS) analysis and identification in order to immediately characterize the unidentified active metabolites in fermentation broth.</p></div>\",\"PeriodicalId\":16891,\"journal\":{\"name\":\"Journal of proteomics\",\"volume\":\"303 \",\"pages\":\"Article 105228\"},\"PeriodicalIF\":2.8000,\"publicationDate\":\"2024-06-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of proteomics\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S187439192400160X\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of proteomics","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S187439192400160X","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
LC-MS/MS profiling and analysis of Bacillus licheniformis extracellular proteins for antifungal potential against Candida albicans
Candida albicans, a significant human pathogenic fungus, employs hydrolytic proteases for host invasion. Conventional antifungal agents are reported with resistance issues from around the world. This study investigates the role of Bacillus licheniformis extracellular proteins (ECP) as effective antifungal peptides (AFPs). The aim was to identify and characterize the ECP of B. licheniformis through LC-MS/MS and bioinformatics analysis. LC-MS/MS analysis identified 326 proteins with 69 putative ECP, further analyzed in silico. Of these, 21 peptides exhibited antifungal properties revealed by classAMP tool and are predominantly anionic. Peptide-protein docking revealed interactions between AFPs like Peptide chain release factor 1 (Q65DV1_Seq1: SASEQLSDAK) and Putative carboxy peptidase (Q65IF0_Seq7: SDSSLEDQDFILESK) with C. albicans virulent SAP5 proteins (PDB ID 2QZX), forming hydrogen bonds and significant Pi-Pi interactions. The identification of B. licheniformis ECP is the novelty of the study that sheds light on their antifungal potential. The identified AFPs, particularly those interacting with bonafide pharmaceutical targets SAP5 of C. albicans represent promising avenues for the development of antifungal treatments with AFPs that could be the pursuit of a novel therapeutic strategy against C. albicans.
Significance of study
The purpose of this work was to carry out proteomic profiling of the secretome of B. licheniformis. Previously, the efficacy of Bacillus licheniformis extracellular proteins against Candida albicans was investigated and documented in a recently communicated manuscript, showcasing the antifungal activity of these proteins. In order to achieve high-throughput identification of ES (Excretory-secretory) proteins, the utilization of liquid chromatography tandem mass spectrometry (LC-MS) was utilized. There was a lack of comprehensive research on AFPs in B. licheniformis, nevertheless. The proteins secreted by B. licheniformis in liquid medium were initially discovered using liquid chromatography-tandem mass spectrometry (LC-MS) analysis and identification in order to immediately characterize the unidentified active metabolites in fermentation broth.
期刊介绍:
Journal of Proteomics is aimed at protein scientists and analytical chemists in the field of proteomics, biomarker discovery, protein analytics, plant proteomics, microbial and animal proteomics, human studies, tissue imaging by mass spectrometry, non-conventional and non-model organism proteomics, and protein bioinformatics. The journal welcomes papers in new and upcoming areas such as metabolomics, genomics, systems biology, toxicogenomics, pharmacoproteomics.
Journal of Proteomics unifies both fundamental scientists and clinicians, and includes translational research. Suggestions for reviews, webinars and thematic issues are welcome.