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Review
. 2013 Dec 9:4:353.
doi: 10.3389/fmicb.2013.00353.

Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance

Fernanda Guilhelmelli  1 , Nathália Vilela  1 , Patrícia Albuquerque  1 , Lorena da S Derengowski  1 , Ildinete Silva-Pereira  1 , Cynthia M Kyaw  2
Affiliations
Review

Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance

Fernanda Guilhelmelli et al. Front Microbiol. .

Abstract

Antimicrobial peptides (AMPs) are natural antibiotics produced by various organisms such as mammals, arthropods, plants, and bacteria. In addition to antimicrobial activity, AMPs can induce chemokine production, accelerate angiogenesis, and wound healing and modulate apoptosis in multicellular organisms. Originally, their antimicrobial mechanism of action was thought to consist solely of an increase in pathogen cell membrane permeability, but it has already been shown that several AMPs do not modulate membrane permeability in the minimal lethal concentration. Instead, they exert their effects by inhibiting processes such as protein and cell wall synthesis, as well as enzyme activity, among others. Although resistance to these molecules is uncommon several pathogens developed different strategies to overcome AMPs killing such as surface modification, expression of efflux pumps, and secretion of proteases among others. This review describes the various mechanisms of action of AMPs and how pathogens evolve resistance to them.

Keywords: antimicrobial peptides; bacterial; mechanism of action; mechanism of resistance; membrane permeability and intracellular targets.

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References

    1. Abi Khattar Z., Rejasse A., Destoumieux-Garzon D., Escoubas J. M., Sanchis V., Lereclus D., et al. (2009). The dlt operon of Bacillus cereus is required for resistance to cationic antimicrobial peptides and for virulence in insects. J. Bacteriol. 191 7063–707310.1128/JB.00892-09 - DOI - PMC - PubMed
    1. Aerts A. M., Bammens L., Govaert G., Carmona-Gutierrez D., Madeo F., Cammue B. P., et al. (2011). The antifungal plant defensin HsAFP1 from Heuchera sanguinea induces apoptosis in Candida albicans. Front. Microbiol. 2:47.10.3389/fmicb.2011.00047 - DOI - PMC - PubMed
    1. Anbanandam A., Albarado D. C., Tirziu D. C., Simons M., Veeraraghavan S. (2008). Molecular basis for proline- and arginine-rich peptide inhibition of proteasome. J. Mol. Biol. 384 219–22710.1016/j.jmb.2008.09.021 - DOI - PMC - PubMed
    1. Andra J., Goldmann T., Ernst C. M., Peschel A., Gutsmann T. (2011). Multiple peptide resistance factor (MprF)-mediated resistance of Staphylococcus aureus against antimicrobial peptides coincides with a modulated peptide interaction with artificial membranes comprising lysyl-phosphatidylglycerol. J. Biol. Chem. 286 18692–1870010.1074/jbc.M111.226886 - DOI - PMC - PubMed
    1. Bachrach G., Altman H., Kolenbrander P. E., Chalmers N. I., Gabai-Gutner M., Mor A., et al. (2008). Resistance of Porphyromonas gingivalis ATCC 33277 to direct killing by antimicrobial peptides is protease independent. Antimicrob. Agents Chemother. 52 638–64210.1128/AAC.01271-07 - DOI - PMC - PubMed

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