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Abstract
Antimicrobial peptides (AMPs) are a diverse group of short, cationic peptides which are naturally occurring molecules in the first-line defense of most living organisms. They represent promising candidates for the treatment of pathogenic microorganisms. Snakin-2 (SN2) from tomato (Solanum lycopersicum) is stabilized through six intramolecular disulphide bridges; it shows broad-spectrum antimicrobial activity against bacteria and fungi, and it agglomerates single cells prior to killing. In this study, we further characterized SN2 by providing time-kill curves and corresponding growth inhibition analysis of model organisms, such as E. coli or B. subtilis. SN2 was produced recombinantly in E. coli with thioredoxin as fusion protein, which was removed after affinity purification by proteolytic digestion. Furthermore, the target specificity of SN2 was investigated by means of hemolysis and hemagglutination assays; its effect on plant cell membranes of isolated protoplasts was investigated by microscopy. SN2 shows a non-specific pore-forming effect in all tested membranes. We suggest that SN2 could be useful as a preservative agent to protect food, pharmaceuticals, or cosmetics from decomposition by microbes.
Highlights
Multidrug-resistant microorganisms, which cause thousands of deaths each year, have become more prominent in recent decades, and it is necessary to find and investigate new types of antimicrobial agents to counteract these pathogens
For E. coli, it was previously reported that the 2× MIC is bactericidal (Herbel, Schäfer & Wink, 2015); this was observed in the kinetics analysis in which, after 24 h, no viable cells could be detected
We did not use a label for SN2, as for example GPF could be used, because the activity of SN2 is dramatically reduced if it is fused to another protein, as we found for the expressed fusion protein consisting out of thioredoxin and SN2 (Trx-SN2)
Summary
Multidrug-resistant microorganisms, which cause thousands of deaths each year, have become more prominent in recent decades, and it is necessary to find and investigate new types of antimicrobial agents to counteract these pathogens. Due to the diversity of potential pathogens, many host defense mechanisms, including antimicrobial peptides (AMPs), have evolved upon infection. These ribosomally synthesized natural antibiotics occur ubiquitously throughout prokaryotes, insects, plants, and animals and can be classified according to various characteristics like biological function, peptide properties as net charge or hydrophobicity, 3D structure, covalent binding patterns, molecular targets, or biological source (Tam et al, 2015). AMPs are a diverse group, but the majority share characteristics like cationic net charge, small molecular weight, and a similar antimicrobial effect, amino acid sequences and their consequent secondary structures are likewise highly diverse (Jenssen, Hamill & Hancock, 2006).
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