Mechanism of antimicrobial action of indolicidin

Subbalakshmi, C

doi:10.1016/s0378-1097(98)00008-1

Cited by 76 publications

(96 citation statements)

References 19 publications

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“…[12,57,[59][60][61] The AMPs indolicitin and buforin II have also demonstrated the ability to bind directly to DNA. [34,62] It has been shown that wheat seed purothionin is able to block in vitro DNA synthesis through inhibition of the enzyme ribonucleotide reductase. It has been proposed that inhibition of DNA synthesis may explain the toxic effect of thionins against mammalian cells.…”

Section: Discussionmentioning

confidence: 99%

Antimicrobial activity and mechanism of action of a thionin‐like peptide from Capsicum annuum fruits and combinatorial treatment with fluconazole against Fusarium solani

et al. 2017

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Many Fusarium species are able to cause severe infections in plants as well as in animals and humans. Therefore, the discovery of new antifungal agents is of paramount importance. CaThi belongs to the thionins, which are cationic peptides with low molecular weights (∼5 kDa) that have toxic effects against various microorganisms. Herein, we study the mechanism of action of CaThi and its combinatory effect with fluconazole (FLC) against Fusarium solani. The mechanism of action of CaThi was studied by growth inhibition, viability, plasma membrane permeabilization, ROS induction, caspase activation, localization, and DNA binding capability, as assessed with Sytox green, DAB, FITC-VAD-FMK, CaThi-FITC, and gel shift assays. The combinatory effect of CaThi and FLC was assessed using a growth inhibition assay. Our results demonstrated that CaThi present a dose dependent activity and at the higher used concentration (50 µg mL ) inhibits 83% of F. solani growth, prevents the formation of hyphae, permeabilizes membranes, induces endogenous H O , activates caspases, and localizes intracellularly. CaThi combined with FLC, at concentrations that alone do not inhibit F. solani, result in 100% death of F. solani when combined. The data presented in this study demonstrate that CaThi causes death of F. solani via apoptosis; an intracellular target may also be involved. Combined treatment using CaThi and FLC is a strong candidate for studies aimed at improved targeting of F. solani. This strategy is of particular interest because it minimizes selection of resistant microorganisms.

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Section: Discussionmentioning

confidence: 99%

Antimicrobial activity and mechanism of action of a thionin‐like peptide from Capsicum annuum fruits and combinatorial treatment with fluconazole against Fusarium solani

et al. 2017

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“…Such filamentation was reported to be the result of binding to the intracellular macromolecules including DNA (puroindoline and indolicidin), RNA polymerase (microcin J25), and ClpP protease (acyldepsipeptides). [13][14][15][16] We thus speculated that RO-A would also exhibit its antimicrobial activity by interacting with intracellular macromolecules after penetrating the cellular membrane.…”

Section: Observation Of E Coli Morphology Treated With Ro-amentioning

confidence: 99%

Collagen‐like antimicrobial peptides

et al. 2016

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Combinatorial library composed of rigid rod-like peptides with a triple-helical scaffold was constructed. The component peptides were designed to have various combinations of basic and neutral (or hydrophobic) amino acid residues based on collagen-like (Gly-Pro-Yaa)-repeating sequences, inspired from the basic and amphiphilic nature of naturally occurring antimicrobial peptides. Screening of the peptide pools resulted in identification of antimicrobial peptides. A structure-activity relationship study revealed that the position of Arg-cluster at N-terminus and cystine knots at C-terminus in the triple helix significantly contributed to the antimicrobial activity. The most potent peptide RO-A showed activity against Gram-negative Escherichia coli and Gram-positive Bacillus subtilis. In addition, Escherichia coli exposed to RO-A resulted in abnormal elongation of the cells. RO-A was also shown to have remarkable stability in human serum and low cytotoxicity to mammalian cells. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 453-459, 2016.

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“…It has been reported that intracellular genomic DNA is an important target of antimicrobial peptides (13). After interacting with genomic DNAs, a number of antimicrobial peptides interrupt the expression of proteins involved in gene replication and transcription, resulting in bacterial death (28,29). In this study, the cell membrane permeabilization assay suggests that the membrane is the preliminary target of AN5-1 and AN5-1 disrupts both the outer and inner bacterial membranes.…”

Section: Discussionmentioning

confidence: 72%

Production of an Antimicrobial Peptide AN5‐1 in Escherichia coli and its Dual Mechanisms Against Bacteria

Huang

Chen

2014

Chem Biol Drug Des

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AN5-1 (YSKSLPLSVLNP) is an antimicrobial peptide isolated from the fermentation broth of Paenibacillus alvei strain AN5 (J Ind Microb Biotechnol 2013; 40: 571-9). In this study, we report the application of ubiquitin fusion technology to the expression and purification of AN5-1. Minimum inhibitory concentration (MIC) and measurement of hemolytic activity (MHC) were measured to confirm the biological activities of the expressed AN5-1. Bacterial cell membrane permeabilization was investigated to show the interaction between the AN5-1 and the bacterial cytoplasmic membrane. Furthermore, intracellular activities of the AN5-1 were determined by genomic DNA interaction assays. The results revealed AN5-1 damaging bacterial membranes and binding to bacterial genomic DNA to inhibit cellular functions, suggesting that it has multiple intracellular targets in bacteria. The application of ubiquitin fusion technology may be an excellent approach for industrial production to the expression and purification of antimicrobial peptide. Furthermore, AN5-1 was demonstrated as an antimicrobial peptide with great potentials, as bacterial resistance to AN5-1 would be not expected, due to the dual mechanisms of AN5-1 against bacteria.

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Mechanism of antimicrobial action of indolicidin

Cited by 76 publications

References 19 publications

Antimicrobial activity and mechanism of action of a thionin‐like peptide from Capsicum annuum fruits and combinatorial treatment with fluconazole against Fusarium solani

Antimicrobial activity and mechanism of action of a thionin‐like peptide from Capsicum annuum fruits and combinatorial treatment with fluconazole against Fusarium solani

Collagen‐like antimicrobial peptides

Production of an Antimicrobial Peptide AN5‐1 in Escherichia coli and its Dual Mechanisms Against Bacteria

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