Ontology highlight
ABSTRACT:
PROVIDER: PRJEB40969 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| ERR4760490_1.fastq.gz | Fastqsanger.gz | |||
| ERR4760490_2.fastq.gz | Fastqsanger.gz | |||
| ERR4760491_1.fastq.gz | Fastqsanger.gz | |||
| ERR4760491_2.fastq.gz | Fastqsanger.gz | |||
| ERR4760482_1.fastq.gz | Fastqsanger.gz |
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Project description:Migration of antimicrobial resistance genes along the food production chain from raw manure to mushroom
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Project description:Antimicrobial peptides (AMPs) constitute a broad range of bioactive compounds in diverse organisms, including fish. They are effector molecules for the innate immune response, against pathogens, tissue damage and infections. Still, AMPs from African Catfish, Clarias gariepinus skin mucus are largely unexplored despite their possible therapeutic role in combating antimicrobial resistance. In this study, African Catfish Antimicrobial peptides (ACAPs) were identified from the skin mucus of African Catfish, C. gariepinus. Native peptides were extracted from fish mucus scrapings in 10% acetic acid (v/v) and ultra-filtered using 5kDa molecular cut-off membrane. The extract was purified using C18 Solid Phase Extraction. The antibacterial activity was determined using the Agar Well Diffusion method and broth-dilution method utilizing Staphylococcus aureus (ATCC 25923) and Escherichia coli (ATCC 25922). Thereafter, Sephadex G-25 gel filtration was further utilized in bio-guided isolation of the most active fractions prior to peptide identification using Orbitrap Fusion Lumos Tribrid Mass Spectrometry. The skin mucus extracted from African Catfish from all the three major lakes of Uganda exhibited antimicrobial activity on E. coli and S. aureus. Lake Albert’s C. gariepinus demonstrated the best activity with the lowest MIC of 2.84 µg/mL and 0.71 µg/mL on S. aureus and E. coli respectively. Sephadex G-25 peak I mass spectrometry analysis alongside in silico analysis revealed seven short peptides (11-15 amino acid residues) of high antimicrobial scores (0.561-0.905 units). In addition, these peptides had a low molecular weight (1005.57-1622.05 Da), and had percentage hydrophobicity above 54%. Up to four of these antimicrobial peptides demonstrated α-helix structure conformation, rendering them amphipathic. The findings of this study indicate that novel antimicrobial peptides can be sourced from the skin mucus of C. gariepinus. Such antimicrobial peptides are potential alternatives to the traditional antibiotics and can be of great application to food and pharmaceutical industries; however, further studies are still needed to establish their drug-likeness and safety profiles.
2021-12-01 | PXD029193 | Pride
Project description:Food-Food Production Metagenome
| PRJNA999631 | ENA
Project description:Campylobacter spp. cause food-borne illnesses worldwide due to contaminated food and cross-contamination. This is at least partly the result of Campylobacter resistance in the food production chain, as modern food production facilitates the emergence and spread of resistance through intensive use of antimicrobials and international trade in raw materials and food products. The biofilm 'lifestyle' of Campylobacter contributes to this spread as it enables them to withstand stress in the environment both outside and inside the host. Campylobacter adhesion and biofilm formation has major implications for the food industry, where biofilms can be persistent sources of contamination. In our study, we described how the proteome of C. jejuni is affected by the deletion of the luxS gene on the planktonic cell type of C. jejuni, which is the first step of biofilm formation. In C. jejuni, the presence of the luxS gene has been associated with several phenotypes, including intercellular signalling, motility, biofilm formation, host colonisation, virulence, autoagglutination, cellular adherence and invasion, oxidative stress and chemotaxis. Deletion of the luxS gene is associated with a reduction or absence of the above properties compared to wild type (Elvers and Park, 2002; Guerry et al., 2006; He et al., 2008; Jeon et al., 2003; Quiñones et al., 2009; Plummer et al., 2011; Plummer, 2012; Reeser et al., 2007).
2023-01-24 | PXD035008 | Pride
Project description:Antimicrobial peptides (AMPs) are garnering attention as possible alternatives to antibiotics. Here, we describe the antimicrobial properties of epinecidin-1 against multi-drug resistant clinical isolates of P. aeruginosa (P. aeruginosa (R)) and P. aeruginosa from ATCC (P. aeruginosa (19660)) in vivo. The minimum inhibitory concentrations (MICs) of epinecidin-1 against P. aeruginosa (R) and P. aeruginosa (19660) were determined, and compared with those of imipenem. Epinecidin-1 was found to be highly effective at combating peritonitis infection caused by P. aeruginosa (R) or P. aeruginosa (19660) in mouse models, without inducing adverse behavioral effects, or liver or kidney toxicity. Taken together, our results indicate that epinecidin-1 enhances the survival rate of mice infected with the bacterial pathogen P. aeruginosa through both antimicrobial and immunomodulatory effects. RNA from mice treated with epinecidin-1 were individually compared to RNA from PBS control mice.
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