Dataset Information

Fate and Biological Activity of the Antimicrobial Lasso Peptide Microcin J25 Under Gastrointestinal Tract Conditions.

ABSTRACT: The bacteriocin microcin J25 (MccJ25) inhibits the growth of Gram-negative pathogens including Salmonella and Shigella species, and Escherichia coli. This 21-amino acid peptide has remarkable stability to heat and extreme pH values and resistance to many proteases, thanks to a characteristic lasso structure. In this study, we used the dynamic simulator TIM-1 as gastro-intestinal tract model to evaluate the stability and antibacterial activity of MccJ25 during passage through the proximal portion of the human gastrointestinal tract. MccJ25 concentration was measured in the different simulator sections by HPLC, and inhibition of Salmonella enterica serotype Enteritidis was evaluated using qualitative and quantitative assays. LC-MS/MS analysis and subsequent molecular networking analysis on the Global Natural Product Social Molecular Networking platform (GNPS) and analysis of the peptide degradation in the presence of proteolytic enzymes mimicking the gastro-intestinal conditions permitted to delineate the fate of MccJ25 through identification of the main degradation products. MccJ25 was relatively stable under gastric conditions, but degraded rapidly in the compartment mimicking the duodenum, notably in the presence of pancreatin. Among pancreatin components, elastase I appeared primarily responsible for MccJ25 breakdown, while ?-chymotrypsin was less efficient.

SUBMITTER: Naimi S

PROVIDER: S-EPMC6085462 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Fate and Biological Activity of the Antimicrobial Lasso Peptide Microcin J25 Under Gastrointestinal Tract Conditions.

Naimi Sabrine S Zirah Séverine S Hammami Riadh R Fernandez Benoît B Rebuffat Sylvie S Fliss Ismail I

Frontiers in microbiology 20180803

The bacteriocin microcin J25 (MccJ25) inhibits the growth of Gram-negative pathogens including Salmonella and Shigella species, and Escherichia coli. This 21-amino acid peptide has remarkable stability to heat and extreme pH values and resistance to many proteases, thanks to a characteristic lasso structure. In this study, we used the dynamic simulator TIM-1 as gastro-intestinal tract model to evaluate the stability and antibacterial activity of MccJ25 during passage through ...[more]

PMID: 30123205

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Project description:Poison of intestinal induce severe health problems in human infants and young animals due to contaminating foods and feedstuffs. With the emergence of public health concerns and high-speed diffuse of drug-opposition of bacteria, the adoption of antimicrobial peptides as potential candidates in treating pathogen infections raised up. Nature Microcin J25 (MccJ25), a class of lasso peptides separated from a fecal strain of E. coli, has been replied to display powerful antimicrobial behavior. Herein, the study was to assess the usefulness of biogenic MccJ25 in the prophylaxis of ETEC K88 infection in IPEC-J2 cells. In vitro antimicrobial activity against ETEC K88 and cytotoxicity of biogenic MccJ25 were determined first. To further understand how biogenic MccJ25 mediates its impact, ETEC K88 adhesion in cells, membrane permeability [as indicated by reduced release of lactate dehydrogenase (LDH)], transepithelial electrical resistance (TEER), barrier function, and proinflammatory cytokines levels were determined in IPEC-J2 cells after treatment with biogenic MccJ25 and challenge with ETEC K88. Biogenic MccJ25 had a minimum inhibitory concentration of 0.25 μg/mL against ETEC K88, decreased ETEC K88 adhesion in cells and did not cause cytotoxicity toward cells. Furthermore, biogenic MccJ25 protects against ETEC-induced barrier dysfunction by increasing the TEER, decreasing the LDH and promoting tight junction proteins (TJPs) by promoting the assembly of occludin and claudin-1 in the tight junction complex. Biogenic MccJ25 was further found to relieve inflammation responses through modulation of interleukine-6, IL-8 and tumor necrosis factor-α levels via inhibition of mitogen-activated protein kinase (MAPK) and nuclear factor κB activation. In summary, biogenic MccJ25 can protects against ETEC K88-induced intestinal damage and inflammatory response, recommend the hidden adoption of biogenic MccJ25 as a novel prophylactic agent to reduce pathogen infection in animals, food or humans.

Project description:Natural microcin J25 (MccJ25) represent promising alternatives to traditional antibiotics for the treatment of drug-resistant infections. However, little is known about the antibacterial activity of recombinant MccJ25 against foodborne pathogens. Here, the activity of recombinant MccJ25 was examined using a matrix of conditions in order to assess the efficacy of recombinant MccJ25 as a mitigation against foodborne pathogens, such as Salmonella species and Escherichia coli (E. coli) O157:H7. Results showed that recombinant MccJ25 displayed excellent antimicrobial activity against these foodborne pathogens, including clinical isolates of Salmonella and E. coli, as well as clinical antibiotic-resistant Salmonella and E. coli isolates with different minimal inhibitory concentrations. In addition, antimicrobial activity curves and Live/Dead assay evidenced that recombinant MccJ25 harbors strong bactericidal activity against Salmonella and E. coli O157:H7. Notably, recombinant MccJ25 also had great potency and induced fast mortality against different growth phase of Salmonella and E. coli. The stability analysis results showed that the activity of recombinant MccJ25 was not influenced by temperatures as high as 121°C. Varying the pH from 2.0 to 9.0 did not appear to affect the activity of recombinant MccJ25. Under the challenge of several proteases, simulated gastrointestinal fluids and serum, recombinant MccJ25 still maintained exceptionally strong antimicrobial activity. Significant reductions in Salmonella Pullorum levels were also achieved in food biological environments, such as milk, egg and meat. Moreover, we demonstrated that recombinant MccJ25 appeared to act by inducing membrane breaks, thinning, and disintegration in the Salmonella Pullorum cytoplasmic membrane. Taken together, these results indicated that recombinant MccJ25 could be an effective alternative for mitigating and prevention of Salmonella and E. coli infection in food, animal and agriculture applications.

Dataset Information

Fate and Biological Activity of the Antimicrobial Lasso Peptide Microcin J25 Under Gastrointestinal Tract Conditions.

Publications

Fate and Biological Activity of the Antimicrobial Lasso Peptide Microcin J25 Under Gastrointestinal Tract Conditions.

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