ArticleAntimicrobial agents and chemotherapy2016
A Novel RNase 3/ECP Peptide for Pseudomonas aeruginosa Biofilm Eradication That Combines Antimicrobial, Lipopolysaccharide Binding, and Cell-Agglutinating Activities.
Article in Antimicrobial agents and chemotherapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 57 citations in OpenAlex.
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- Antibiotic Resistant Biofilms and the Quest for Novel Therapeutic Strategies.Indian journal of microbiology · 2024Review
- Blapstin, a Diapause-Specific Peptide-Like Peptide from the Chinese Medicinal BeetleMicrobiology spectrum · 2023Article
- A novel antimicrobial peptide YS12 isolated from Bacillus velezensis CBSYS12 exerts anti-biofilm properties against drug-resistant bacteria.Bioprocess and biosystems engineering · 2023Article
- Biofilm Lifestyle in Recurrent Urinary Tract Infections.Life (Basel, Switzerland) · 2023Review
- Nationwide survey of refractory asthma with bronchiectasis by inflammatory subtypes.Respiratory research · 2022Article
- A Novel Cryptic Clostridial Peptide That Kills Bacteria by a Cell Membrane Permeabilization Mechanism.Microbiology spectrum · 2022Article
- Essential Role of Enzymatic Activity in the Leishmanicidal Mechanism of the Eosinophil Cationic Protein (RNase 3).ACS infectious diseases · 2022Article
- Recent Strategies to Combat Biofilms Using Antimicrobial Agents and Therapeutic Approaches.Pathogens (Basel, Switzerland) · 2022Review
- In Vivo Evaluation of ECP Peptide Analogues for the Treatment ofBiomedicines · 2022Article
- Exploring the RNase A scaffold to combine catalytic and antimicrobial activities. Structural characterization of RNase 3/1 chimeras.Frontiers in molecular biosciences · 2022Article
- Antibiofilm activity of host defence peptides: complexity provides opportunities.Nature reviews. Microbiology · 2021Review
- Enhancement of Antibiofilm Activity of Ciprofloxacin againstAntibiotics (Basel, Switzerland) · 2021Article
- Rationally Modified Antimicrobial Peptides from the N-Terminal Domain of Human RNase 3 Show Exceptional Serum Stability.Journal of medicinal chemistry · 2021Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eradication of established biofilm communities of pathogenic Gram-negative species is one of the pending challenges for the development of new antimicrobial agents. In particular, Pseudomonas aeruginosa is one of the main dreaded nosocomial species, with a tendency to form organized microbial communities that offer an enhanced resistance to conventional antibiotics. We describe here an engineered antimicrobial peptide (AMP) which combines bactericidal activity with a high bacterial cell agglutination and lipopolysaccharide (LPS) affinity. The RN3(5-17P22-36) peptide is a 30-mer derived from the eosinophil cationic protein (ECP), a host defense RNase secreted by eosinophils upon infection, with a wide spectrum of antipathogen activity. The protein displays high biofilm eradication activity that is not dependent on its RNase catalytic activity, as evaluated by using an active site-defective mutant. On the other hand, the peptide encompasses both the LPS-binding and aggregation-prone regions from the parental protein, which provide the appropriate structural features for the peptide's attachment to the bacterial exopolysaccharide layer and further improved removal of established biofilms. Moreover, the peptide's high cationicity and amphipathicity promote the cell membrane destabilization action. The results are also compared side by side with other reported AMPs effective against either planktonic and/or biofilm forms of Pseudomonas aeruginosa strain PAO1. The ECP and its derived peptide are unique in combining high bactericidal potency and cell agglutination activity, achieving effective biofilm eradication at a low micromolar range. We conclude that the designed RN3(5-17P22-36) peptide is a promising lead candidate against Gram-negative biofilms.
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