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Characterization of Cetacean Proline-Rich Antimicrobial Peptides Displaying Activity against ESKAPE Pathogens
- Source :
- International Journal of Molecular Sciences, Volume 21, Issue 19, International Journal of Molecular Sciences, Vol 21, Iss 7367, p 7367 (2020)
- Publication Year :
- 2020
- Publisher :
- MDPI AG, 2020.
-
Abstract
- Proline-rich antimicrobial peptides (PrAMPs) may be a valuable weapon against multi-drug resistant pathogens, combining potent antimicrobial activity with low cytotoxicity. We have identified novel PrAMPs from five cetacean species (cePrAMPs), and characterized their potency, mechanism of action and in vitro cytotoxicity. Despite the homology between the N-terminal of cePrAMPs and the bovine PrAMP Bac7, some differences emerged in their sequence, activity spectrum and mode of action. CePrAMPs with the highest similarity with the Bac7(1-35) fragment inhibited bacterial protein synthesis without membrane permeabilization, while a second subgroup of cePrAMPs was more membrane-active but less efficient at inhibiting bacterial translation. Such differences may be ascribable to differences in presence and positioning of Trp residues and of a conserved motif seemingly required for translation inhibition. Unlike Bac7(1-35), which requires the peptide transporter SbmA for its uptake, the activity of cePrAMPs was mostly independent of SbmA, regardless of their mechanism of action. Two peptides displayed a promisingly broad spectrum of activity, with minimal inhibiting concentration MIC &le<br />4 &micro<br />M against several bacteria of the ESKAPE group, including Pseudomonas aeruginosa and Enterococcus faecium. Our approach has led us to discover several new peptides<br />correlating their sequences and mechanism of action will provide useful insights for designing optimized future peptide-based antibiotics.
- Subjects :
- antimicrobial peptide
protein synthesis
medicine.medical_treatment
Peptide
Antimicrobial peptide
Cathelicidin
Cetacea
ESKAPE
Membrane permeabilization
Proline-rich
Protein synthesis
lcsh:Chemistry
Sequence Analysis, Protein
Candida albicans
cathelicidin
Protein biosynthesis
lcsh:QH301-705.5
Spectroscopy
chemistry.chemical_classification
0303 health sciences
General Medicine
Antimicrobial
Anti-Bacterial Agents
Computer Science Applications
Biochemistry
medicine.symptom
Pore Forming Cytotoxic Proteins
Antimicrobial peptides
Microbial Sensitivity Tests
Article
Catalysis
Inorganic Chemistry
03 medical and health sciences
Cathelicidins
Prokaryotic translation
medicine
Animals
Physical and Theoretical Chemistry
Mode of action
Molecular Biology
030304 developmental biology
Bacteria
030306 microbiology
Organic Chemistry
lcsh:Biology (General)
lcsh:QD1-999
Mechanism of action
chemistry
Cattle
proline-rich
membrane permeabilization
Sequence Alignment
Antimicrobial Cationic Peptides
Subjects
Details
- ISSN :
- 14220067
- Volume :
- 21
- Database :
- OpenAIRE
- Journal :
- International Journal of Molecular Sciences
- Accession number :
- edsair.doi.dedup.....5415673d3421b403590af1891351dd39