Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Brogden, Kim A.

doi:10.1038/nrmicro1098

Cited by 5,829Antimicrobial Peptides and ActivitiesAntimicrobial agents and applicationsInvertebrate Immune Response Mechanisms

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Brogden, Kim A.·2005·Nature Reviews Microbiology

DOI 10.1038/nrmicro1098

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Abstract

Antimicrobial peptides are an abundant and diverse group of molecules that are produced by many tissues and cell types in a variety of invertebrate, plant and animal species. Their amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert into membrane bilayers to form pores by 'barrel-stave', 'carpet' or 'toroidal-pore' mechanisms. Although these models are helpful for defining mechanisms of antimicrobial peptide activity, their relevance to how peptides damage and kill microorganisms still need to be clarified. Recently, there has been speculation that transmembrane pore formation is not the only mechanism of microbial killing. In fact several observations suggest that translocated peptides can alter cytoplasmic membrane septum formation, inhibit cell-wall synthesis, inhibit nucleic-acid synthesis, inhibit protein synthesis or inhibit enzymatic activity. In this review the different models of antimicrobial-peptide-induced pore formation and cell killing are presented.

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Many AMPs are small cationic peptides binding to and interacting with the negatively charged membranes of microbes and are thereby able to kill the microbe through membrane disruption, whereas other AMPs inhibit bacterial metabolism or growth.
“Many AMPs are small cationic peptides binding to and interacting with the negatively charged membranes of microbes and are thereby able to kill the microbe through membrane disruption, whereas other AMPs inhibit bacterial metabolism or growth.31,32”
From The Innate Immune System in Acute and Chronic Wounds (2016) · cites this paper as [31]

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Purification and Properties of Proline-Rich Antimicrobial Peptides from Sheep and Goat Leukocytes
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The Androgen-Regulated Epididymal Sperm-Binding Protein, Human β-Defensin 118 (DEFB118) (Formerly ESC42), Is an Antimicrobial β-Defensin
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Small, anionic, and charge-neutralizing propeptide fragments of zymogens are antimicrobial
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Magainin 2 amide and analogues Antimicrobial activity, membrane depolarization and susceptibility to proteolysis
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Channel-forming Membrane Permeabilization by an Antibacterial Protein, Sapecin
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Solid-State NMR Investigation of the Selective Perturbation of Lipid Bilayers by the Cyclic Antimicrobial Peptide RTD-1
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Modulation of the Activity of Secretory Phospholipase A 2 by Antimicrobial Peptides
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Differences in the Concentrations of Small, Anionic, Antimicrobial Peptides in Bronchoalveolar Lavage Fluid and in Respiratory Epithelia of Patients with and without Cystic Fibrosis
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Detection of Anionic Antimicrobial Peptides in Ovine Bronchoalveolar Lavage Fluid and Respiratory Epithelium
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Anion pores from magainins and related defensive peptides
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SPAG11/isoform HE2C, an atypical anionic β-defensin-like peptide
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Release of aqueous contents from phospholipid vesicles induced by cecropin A (1–8)‐magainin 2 (1–12) hybrid and its analogues
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Interaction of Gram-Negative Bacteria with the Lysosomal Fraction of Polymorphonuclear Leukocytes II. Changes in the Cell Envelope of Escherichia coli
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Inflammatory bowel disease: cause and immunobiology
Baumgart, D. C., & Carding, S. R. (2007) · The Lancet · doi:10.1016/s0140-6736(07)60750-8 · Cited by 2,147 · see citing works
QSAR Modeling: Where have you been? Where are you going to?
Cherkasov, A., Muratov, E. N., Fourches, D., Varnek, A., Baskin, I. I., Cronin, M., Dearden, J., Gramatica, P., Martin, Y. C., Todeschini, R., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4004285 · Cited by 2,164 · see citing works
LL-37, the only human member of the cathelicidin family of antimicrobial peptides
Dürr, U. H. N., Sudheendra, U. S., & Ramamoorthy, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.030 · Cited by 1,049 · see citing works
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Tiwari, B. K., Valdramidis, V. P., O’ Donnell, C. P., Muthukumarappan, K., Bourke, P., & Cullen, P. J. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf900668n · Cited by 851 · see citing works
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Kim, S., Covington, A., & Pamer, E. G. (2017) · Immunological Reviews · doi:10.1111/imr.12563 · Cited by 741 · see citing works
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Sánchez, A., & Vázquez, A. (2017) · Food Quality and Safety · doi:10.1093/fqs/fyx006 · Cited by 868 · see citing works
CAMP: a useful resource for research on antimicrobial peptides.
Thomas, S., Karnik, S., Barai, R. S., Jayaraman, V. K., & Idicula-Thomas, S. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp1021 · Cited by 462 · see citing works
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Marsh, P. D., Do, T., Beighton, D., & Devine, D. A. (2016) · Periodontology 2000 · doi:10.1111/prd.12098 · Cited by 381 · see citing works
Antimicrobial peptides and plant disease control
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AVPpred: collection and prediction of highly effective antiviral peptides.
Thakur, N., Qureshi, A., & Kumar, M. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks450 · Cited by 324 · see citing works
Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines
Pessione, E., & Cirrincione, S. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00876 · Cited by 333 · see citing works
Lysosomal killing of <i>Mycobacterium</i> mediated by ubiquitin-derived peptides is enhanced by autophagy
Alonso, S., Pethe, K., Russell, D. G., & Purdy, G. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700036104 · Cited by 318 · see citing works
β-Hairpin Peptidomimetics: Design, Structures and Biological Activities
Robinson, J. A. (2008) · Accounts of Chemical Research · doi:10.1021/ar700259k · Cited by 321 · see citing works
Natural roles of antimicrobial peptides in microbes, plants and animals
Maróti, G., Kereszt, A., Kondorosi, É., & Mergaert, P. (2011) · Research in Microbiology · doi:10.1016/j.resmic.2011.02.005 · Cited by 298 · see citing works
The Innate Immune System in Acute and Chronic Wounds
MacLeod, A. S., & Mansbridge, J. N. (2016) · Advances in Wound Care · doi:10.1089/wound.2014.0608 · Cited by 289 · see citing works
“Many AMPs are small cationic peptides binding to and interacting with the negatively charged membranes of microbes and are thereby able to kill the microbe through membrane disruption, whereas other AMPs inhibit bacterial metabolism or growth.(31,32) In the case of infection, inflammation, or injury, many AMPs in the…”
Background
Staphylococcus epidermidis Antimicrobial δ-Toxin (Phenol-Soluble Modulin-γ) Cooperates with Host Antimicrobial Peptides to Kill Group A Streptococcus
Cogen, A. L., Yamasaki, K., Muto, J., Sanchez, K. M., Crotty Alexander, L., Tanios, J., Lai, Y., Kim, J. E., Nizet, V., & Gallo, R. L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008557 · Cited by 245 · see citing works
Vinegar Functions on Health: Constituents, Sources, and Formation Mechanisms
Chen, H., Chen, T., Giudici, P., & Chen, F. (2016) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12228 · Cited by 232 · see citing works
β-Lactoglobulin as source of bioactive peptides.
Hernández-Ledesma, B., Recio, I., & Amigo, L. (2008) · Amino Acids · doi:10.1007/s00726-007-0585-1 · Cited by 210 · see citing works
Identification and Rational Design of Novel Antimicrobial Peptides for Plant Protection
Marcos, J. F., Muñoz, A., Pérez-Payá, E., Misra, S., & López-García, B. (2008) · Annual Review of Phytopathology · doi:10.1146/annurev.phyto.121307.094843 · Cited by 205 · see citing works
Human Antimicrobial Peptide LL-37 Inhibits Adhesion of Candida albicans by Interacting with Yeast Cell-Wall Carbohydrates
Tsai, P.-W., Yang, C.-Y., Chang, H.-T., & Lan, C.-Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017755 · Cited by 175 · see citing works
Antimicrobial peptides: promising compounds against pathogenic microorganisms
Cruz, J., Ortiz, C., Guzmán, F., Fernández-Lafuente, R., & Torres, R. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140217110155 · Cited by 166 · see citing works
Antioxidant Peptidomics Reveals Novel Skin Antioxidant System
Yang, H., Wang, X., Liu, X., Wu, J., Liu, C., Gong, W., Zhao, Z., Hong, J., Lin, D., Wang, Y., et al. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800297-mcp200 · Cited by 156 · see citing works
Massive protein import into the early-evolutionary-stage photosynthetic organelle of the amoeba Paulinella chromatophora
Singer, A., Poschmann, G., Mühlich, C., Valadez-Cano, C., Hänsch, S., Hüren, V., Rensing, S. A., Stühler, K., & Nowack, E. C. M. (2017) · Current Biology · doi:10.1016/j.cub.2017.08.010 · Cited by 116 · see citing works
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Authors: Brogden, K. A.
Affiliations: University of Iowa (US)
Corresponding author: Brogden, Kim A.
ORCID: Brogden, Kim A.
Venue: Nature Reviews Microbiology
Publisher: Springer Science and Business Media LLC
Published: 2005-03
Volume: 3
Issue: 3
Pages: 238-250
ISSN: 1740-1526 (ISSN-L)
1740-1534
DOI: 10.1038/nrmicro1098
OpenAlex: W1989998611
Cited by: 5,829
References: 163
Citations by year: 2026: 225 · 2025: 260 · 2024: 261 · 2023: 273 · 2022: 363 · 2021: 394 · 2020: 400 · 2019: 353 · 2018: 345 · 2017: 360 · 2016: 342 · 2015: 327 · 2014: 296 · 2013: 291 · 2012: 275
FWCI: 15.04
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Microbiology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Dental and Craniofacial Research
Topics: Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
Keywords: antimicrobial peptides, pore formation, membrane permeabilization, carpet mechanism, toroidal pores, cell wall synthesis inhibition, nucleic acid synthesis inhibition, protein synthesis inhibition, enzyme inhibition
MeSH terms: Animals, Anti-Bacterial Agents, Bacteria, Cell Membrane, Humans, Permeability, Protein Conformation, Drug Design, Bacterial Physiological Phenomena, Antimicrobial Cationic Peptides, Drug Resistance, Bacterial

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Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

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