Ontology highlight
ABSTRACT:
PROVIDER: PRJNA635166 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR11851864_1.fastq.gz | Fastqsanger.gz | |||
| SRR11851864_2.fastq.gz | Fastqsanger.gz | |||
| SRR11851865_1.fastq.gz | Fastqsanger.gz | |||
| SRR11851865_2.fastq.gz | Fastqsanger.gz | |||
| SRR11851866_1.fastq.gz | Fastqsanger.gz |
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Project description:Lipopeptide biosurfactant producing Bacillus strains have many useful applications in biotechnology and agriculture, based on their emulsifying, surface activity and antimicrobial properties. In the current study, lipopeptide production kinetics, and biocontrol potentials of two new B. velezensis strains, ES1-02 and EFSO2-04 were analyzed and compared with those of commercial strains QST713 and FZB42. ES1-02 and EFSO2-04 showed higher specific growth rates than FZB42, but lower growth rates than QST713. All strains produced surfactin lipopetides, while fengycin production was not observed in ES1-02 and EFSO2-04. Production of fengycin A, B, X and Y were however confirmed in strains QST713 and FZB42. Significant differences were observed in the production of lipopeptides of the iturin family. While ES1-02 and EFSO2-04 produced bacillomycin L, QST713 produced iturin A, and FZB42 produced bacillomycin D. This was in line with the PCR analysis of corresponding genes encoding the identified lipopeptides. Highest surfactin titer of 97.4 mg/L was observed in ES1-02, while QST713 produced highest amount of iturin/bacillomycin (8.5 mg/L). Surfactin isoforms C12 to C17, and iturin/bacillomycin isoforms C11 to C17 were identified by mass spectrometry. ES1-02 and EFSO2-04 showed biocontrol potentials comparable with that of QST713 against Diaporthe spp., while FZB42 showed superior antifungal potentials. Up to 41%, 43%, 47 % and 68.9 % inhibition of D. caulivora were achieved by ES1-02, EFSO2-04, QST713 and FZB42 respectively. Upon exposure to B. velezensis strains, morphological changes to Diaporthe hyphae in form of swellings, distortion, and complete disruption occurred. Interaction of D. longicolla DPC_HOH20 with ES1-02 and EFSO2-04 induced 10-fold and 5-fold increase in surfactin synthesis, respectively. Antagonist interaction with D. longicolla induced significant changes in the proteome of ES1-02 including an increased abundance of several proteins associated with biosynthesis of antimicrobial compounds and fatty acids, while proteins associated with phosphate uptake were decreased in abundance.
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Project description:Daptomycin is a lipopeptide antibiotic that has recently been approved for treatment of Gram-positive bacterial infections. The mode of action of daptomycin is not yet entirely clear. To further understand the mechanism transcriptomic analysis of changes in gene expression in daptomycin-treated Staphylococcus aureus was carried out. The expression profile indicated that cell wall stress stimulon member genes (B. J. Wilkinson, A. Muthaiyan, and R. K. Jayaswal. 2005. Curr. Med. Chem. Anti-Infective Agents 4: 259-276) were significantly induced by daptomycin, and by the cell wall-active antibiotics vancomycin and oxacillin. Comparison of the daptomycin response of a two-component cell wall stress stimulon regulator VraSR mutant, S. aureus KVR, to its parent N315 showed diminished expression of the cell wall stress stimulon in the mutant. Daptomycin has been proposed to cause membrane depolarization, and the transcriptional responses to carbonyl cyanide m-chlorophenylhydrazone (CCCP) and nisin were determined. Transcriptional profiles of the responses to these antimicrobial agents showed significantly different patterns compared to those of the cell wall-active antibiotics, including little or no induction of the cell wall stress stimulon. However, there were a significant number of genes induced by both CCCP and daptomycin that were not induced by oxacillin or vancomycin, such that the daptomycin transcriptome was probably reflecting a membrane depolarizing activity of this antimicrobial also. The results indicate that inhibition of peptidoglycan biosynthesis, either directly or indirectly, and membrane depolarization are parts of the mode of action of daptomycin. Keywords: mode of action, transcriptional profiling
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Project description:Transcriptome analysis of B.subtilis in response to cyclic lipopeptide antibiotic (fusaricidin)
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Project description:To establish the protein expression profile of Ba168, a high-resolution LC-MS/MS proteomic analysis was performed. A total of 1155 proteins were identified from 5233 unique peptides. GO and KEGG analysis revealed that a majority of the proteins were associated with biosynthesis and carbon metabolism pathways, such as biosynthesis of amino acids, peptidoglycan, and antibiotics. Then, we identified the antimicrobial proteins of Ba168. At least 16 potential antimicrobial-activity-related proteins were identified; 11 of these proteins have direct antimicrobial effects, while 5 of these proteins are associated with the formation of antimicrobial substances.
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Project description:Staphylococcus aureus is a leading cause of hospital-associated infections. In addition, highly virulent strains of methicillin-resistant S. aureus (MRSA) are currently spreading outside health care settings. Survival in the human host is largely defined by the ability of S. aureus to resist mechanisms of innate host defense, of which antimicrobial peptides form a key part especially on epithelia and in neutrophil phagosomes. Here we demonstrate that the antimicrobial-peptide sensing system aps of the standard community-associated MRSA strain MW2 controls resistance to cationic antimicrobial peptides. The core of aps-controlled resistance mechanisms comprised the D-alanylation of teichoic acids (dlt operon), the incorporation of cationic lysyl-phosphatidylglycerol (L-PG) in the bacterial membrane (mprF), and the vraF/vraG putative antimicrobial peptide transporter. Further, the observed increased production of L-PG under the influence of cationic antimicrobial peptides was accompanied by the up-regulation of lysine biosynthesis. In noticeable difference to the aps system of S. epidermidis, only selected antimicrobial peptides strongly induced the aps response. Heterologous complementation with the S. epidermidis apsS gene indicated that this is likely caused by differences in the short extracellular loop of ApsS that interacts with the inducing antimicrobial peptide. Our study shows that the antimicrobial peptide sensor system aps is functional in the important human pathogen S. aureus, significant interspecies differences exist in the induction of the aps gene regulatory response, and aps inducibility is clearly distinguishable from effectiveness towards a given antimicrobial peptide. Keywords: Wild type control vs treated vs mutant Wild type untreated in triplicate is compared to wild type treated in triplicate along with three mutants in triplicate with and without treatment of indolicidin, totalling 30 samples
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