Synergistic and Antibiofilm Properties of Ocellatin Peptides Against Multidrug-Resistant
            <i>Pseudomonas Aeruginosa</i>

Bessa, Lucinda J.; Eaton, Peter; Dematei, Anderson; Plácido, Alexandra; Vale, Nuno; Gomes, Paula; Delerue–Matos, Cristina; Leite, J. R.; Gameiro, Paula

doi:10.2217/fmb-2017-0175

Cited by 46 publications

(45 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In all three cases, the inhibition of the biofilm did not result in the destruction of cells or the slowing down of their growth. This is very important because, usually, biofilms are insensitive to antibiotics and the increase in the effectiveness of antibiotics is explained by the ability to inhibit biofilm formation [67][68][69], which could explain why the synergistic effect in the case of F2 fractions was more pronounced for the strain forming the biofilm (ATCC 35984).…”

Section: Discussionmentioning

confidence: 99%

Antimicrobial Activity of Protein Fraction from Naja ashei Venom against Staphylococcus epidermidis

et al. 2020

View full text Add to dashboard Cite

One of the key problems of modern infectious disease medicine is the growing number of drug-resistant and multi-drug-resistant bacterial strains. For this reason, many studies are devoted to the search for highly active antimicrobial substances that could be used in therapy against bacterial infections. As it turns out, snake venoms are a rich source of proteins that exert a strong antibacterial effect, and therefore they have become an interesting research material. We analyzed Naja ashei venom for such antibacterial properties, and we found that a specific composition of proteins can act to eliminate individual bacterial cells, as well as the entire biofilm of Staphylococcus epidermidis. In general, we used ion exchange chromatography (IEX) to obtain 10 protein fractions with different levels of complexity, which were then tested against certified and clinical strains of S. epidermidis. One of the fractions (F2) showed exceptional antimicrobial effects both alone and in combination with antibiotics. The protein composition of the obtained fractions was determined using mass spectrometry techniques, indicating a high proportion of phospholipases A2, three-finger toxins, and L-amino acids oxidases in F2 fraction, which are most likely responsible for the unique properties of this fraction. Moreover, we were able to identify a new group of low abundant proteins containing the Ig-like domain that have not been previously described in snake venoms.

show abstract

Section: Discussionmentioning

confidence: 99%

Antimicrobial Activity of Protein Fraction from Naja ashei Venom against Staphylococcus epidermidis

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Bessa et al [ 45 ] reported that ocellatins isolated from L. pustulatus acted preferentially on clinical isolates of multidrug-resistant P. aeruginosa (MICs 16–256 µg/mL) compared with reference strains (MICs > 520 µg/mL). In particular, ocellatin-PT3 displayed an ability to inhibit biofilm formation (concentrations 4–8 times higher than the MIC) and showed synergistic effects with the antibiotics ciprofloxacin and ceftazidime, so the peptide was proposed as a promising lead molecule for the design and development of novel therapeutic agents against drug-resistant P. aeruginosa biofilms.…”

Section: Discussionmentioning

confidence: 99%

Peptidomic Analysis of Skin Secretions of the Caribbean Frogs Leptodactylus insularum and Leptodactylus nesiotus (Leptodactylidae) Identifies an Ocellatin with Broad Spectrum Antimicrobial Activity

et al. 2020

View full text Add to dashboard Cite

Ocellatins are peptides produced in the skins of frogs belonging to the genus Leptodactylus that generally display weak antimicrobial activity against Gram-negative bacteria only. Peptidomic analysis of norepinephrine-stimulated skin secretions from Leptodactylus insularum Barbour 1906 and Leptodactylus nesiotus Heyer 1994, collected in the Icacos Peninsula, Trinidad, led to the purification and structural characterization of five ocellatin-related peptides from L. insularum (ocellatin-1I together with its (1–16) fragment, ocellatin-2I and its (1–16) fragment, and ocellatin-3I) and four ocellatins from L. nesiotus (ocellatin-1N, -2N, -3N, and -4N). While ocellatins-1I, -2I, and -1N showed a typically low antimicrobial potency against Gram-negative bacteria, ocellatin-3N (GIFDVLKNLAKGVITSLAS.NH2) was active against an antibiotic-resistant strain of Klebsiella pneumoniae and reference strains of Escherichia coli, K. pneumoniae, Pseudomonas aeruginosa, and Salmonella typhimurium (minimum inhibitory concentrations (MICs) in the range 31.25–62.5 μM), and was the only peptide active against Gram-positive Staphylococcus aureus (MIC = 31.25 μM) and Enterococcus faecium (MIC = 62.5 μM). The therapeutic potential of ocellatin-3N is limited by its moderate hemolytic activity (LC50 = 98 μM) against mouse erythrocytes. The peptide represents a template for the design of long-acting, non-toxic, and broad-spectrum antimicrobial agents for targeting multidrug-resistant pathogens.

show abstract

“…The ability of the test compounds to inhibit the biofilm formation by KP010 (a MDR clinical isolate of K. pneumoniae ) was assessed at the respective MIC, 1 / 2 ×MIC and 1 / 4 ×MIC values in tryptic soy broth (TSB) using the crystal violet assay as previously reported [ 36 , 37 ]. Three independent experiments were performed in triplicate for each condition.…”

Section: Methodsmentioning

confidence: 99%

“Clicking” an Ionic Liquid to a Potent Antimicrobial Peptide: On the Route towards Improved Stability

Gomes

Bessa

Correia

et al. 2020

IJMS

Self Cite

View full text Add to dashboard Cite

A covalent conjugate between an antibacterial ionic liquid and an antimicrobial peptide was produced via “click” chemistry, and found to retain the parent peptide’s activity against multidrug-resistant clinical isolates of Gram-negative bacteria, and antibiofilm action on a resistant clinical isolate of Klebsiella pneumoniae, while exhibiting much improved stability towards tyrosinase-mediated modifications. This unprecedented communication is a prelude for the promise held by ionic liquids -based approaches as tools to improve the action of bioactive peptides.

show abstract

Synergistic and Antibiofilm Properties of Ocellatin Peptides Against Multidrug-Resistant Pseudomonas Aeruginosa

Abstract: Ocellatin-PT3 may be promising as a template for the development of novel antimicrobial peptides against P. aeruginosa. [Formula: see text].

Cited by 46 publications

References 32 publications

Antimicrobial Activity of Protein Fraction from Naja ashei Venom against Staphylococcus epidermidis

Antimicrobial Activity of Protein Fraction from Naja ashei Venom against Staphylococcus epidermidis

Peptidomic Analysis of Skin Secretions of the Caribbean Frogs Leptodactylus insularum and Leptodactylus nesiotus (Leptodactylidae) Identifies an Ocellatin with Broad Spectrum Antimicrobial Activity

“Clicking” an Ionic Liquid to a Potent Antimicrobial Peptide: On the Route towards Improved Stability

Contact Info

Product

Resources

About