Bacterial resistance to antimicrobial peptides an evolving phenomenon

Fleitas, Osmel; Agbale, Caleb M; Franco, Octávio Luiz

doi:10.2741/4438

Cited by 11 publications

(3 citation statements)

References 127 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…So far, no multicellular organism has been identified which does not produce antimicrobial peptides. Even over a long time of evolution those host defense molecules have retained their antimicrobial capacity with only minor resistance mechanisms at the microbial target 15,27 . Thus, an improved knowledge of these antibacterial molecules may help to identify novel targets for antimicrobial therapy 28 .…”

Section: Discussionmentioning

confidence: 99%

“…Due to their ancient evolutionary origin and the strong demand for novel antimicrobial strategies, AMPs have been considered as potential antibiotic drug candidates. Mainly because they target “Achilles heels” of microorganisms, only few resistance mechanisms have been evolved over long time 14,15 . Still, large-scale chemical synthesis of defensins containing three native disulphide-bridges has been a challenge and rendered the production expensive.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Proteolytic Degradation of reduced Human Beta Defensin 1 generates a Novel Antibiotic Octapeptide

Wendler

Schroeder

Ehmann

et al. 2019

Sci Rep

View full text Add to dashboard Cite

Microbial resistance against clinical used antibiotics is on the rise. Accordingly, there is a high demand for new innovative antimicrobial strategies. The host-defense peptide human beta-defensin 1 (hBD-1) is produced continuously by epithelial cells and exhibits compelling antimicrobial activity after reduction of its disulphide bridges. Here we report that proteolysis of reduced hBD-1 by gastrointestinal proteases as well as human duodenal secretions produces an eight-amino acid carboxy-terminal fragment. The generated octapeptide retains antibiotic activity, yet with distinct characteristics differing from the full-length peptide. We modified the octapeptide by stabilizing its termini and by using non-natural D-amino acids. The native and modified peptide variants showed antibiotic activity against pathogenic as well as antibiotic-resistant microorganisms, including E . coli , P . aeruginosa and C . albicans . Moreover, in an in vitro C . albicans infection model the tested peptides demonstrated effective amelioration of C . albicans infection without showing cytotoxity on human cells. In summary, protease degradation of hBD-1 provides a yet unknown mechanism to broaden antimicrobial host defense, which could be used to develop defensin-derived therapeutic applications.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Proteolytic Degradation of reduced Human Beta Defensin 1 generates a Novel Antibiotic Octapeptide

Wendler

Schroeder

Ehmann

et al. 2019

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Antimicrobial peptides are a promising alternative to the use of antibiotics and other chemical compounds (7,9,41,42) presenting several advantages, such as limited toxic effects and broad spectrum of antimicrobial properties against bacteria, as well as viruses, fungi, parasites and even anomalous cells. They are also less prone to cause bacterial resistance, but still not totally impervious to that effect (43)(44)(45)(46). Among antimicrobial peptides, hepcidin is of particular interest, especially in teleost fish.…”

Section: Discussionmentioning

confidence: 99%

The Era of Antimicrobial Peptides: Use of Hepcidins to Prevent or Treat Bacterial Infections and Iron Disorders

et al. 2021

View full text Add to dashboard Cite

The current treatments applied in aquaculture to limit disease dissemination are mostly based on the use of antibiotics, either as prophylactic or therapeutic agents, with vaccines being available for a limited number of fish species and pathogens. Antimicrobial peptides are considered as promising novel substances to be used in aquaculture, due to their antimicrobial and immunomodulatory activities. Hepcidin, the major iron metabolism regulator, is found as a single gene in most mammals, but in certain fish species, including the European sea bass (Dicentrarchus labrax), two different hepcidin types are found, with specialized roles: the single type 1 hepcidin is involved in iron homeostasis trough the regulation of ferroportin, the only known iron exporter; and the various type 2 hepcidins present antimicrobial activity against a number of different pathogens. In this study, we tested the administration of sea bass derived hepcidins in models of infection and iron overload. Administration with hamp2 substantially reduced fish mortalities and bacterial loads, presenting itself as a viable alternative to the use of antibiotics. On the other hand, hamp1 seems to attenuate the effects of iron overload. Further studies are necessary to test the potential protective effects of hamp2 against other pathogens, as well as to understand how hamp2 stimulate the inflammatory responses, leading to an increased fish survival upon infection.

show abstract

Combined antimicrobial activity of short peptide and phage-derived endolysin against antibiotic-resistant Salmonella Typhimurium

Kim,

Hasan,

Liao

et al. 2025

Food Microbiology

View full text Add to dashboard Cite

Bacterial resistance to antimicrobial peptides an evolving phenomenon

Cited by 11 publications

References 127 publications

Proteolytic Degradation of reduced Human Beta Defensin 1 generates a Novel Antibiotic Octapeptide

Proteolytic Degradation of reduced Human Beta Defensin 1 generates a Novel Antibiotic Octapeptide

The Era of Antimicrobial Peptides: Use of Hepcidins to Prevent or Treat Bacterial Infections and Iron Disorders

Combined antimicrobial activity of short peptide and phage-derived endolysin against antibiotic-resistant Salmonella Typhimurium

Contact Info

Product

Resources

About