Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii
| Autor: | Monique L. van Hoek, Evelyn J. Hrifko, Ezra M. Chung, Stephanie M. Barksdale |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Microbiology (medical) Acinetobacter baumannii Staphylococcus aureus Erythrocytes Multi drug resistant bacteria 030106 microbiology Antimicrobial peptides Peptide Multi-drug resistant bacteria Microbial Sensitivity Tests medicine.disease_cause Microbiology Protein Structure Secondary 03 medical and health sciences Drug Resistance Multiple Bacterial medicine Escherichia coli Animals Amino Acid Sequence Peptide sequence chemistry.chemical_classification Alligators and Crocodiles Sheep biology Cell Membrane Antimicrobial biology.organism_classification Anti-Bacterial Agents Protein Structure Tertiary Alligator mississippiensis 030104 developmental biology chemistry Pseudomonas aeruginosa Research Article Antimicrobial Cationic Peptides |
| Zdroj: | BMC Microbiology |
| ISSN: | 1471-2180 |
| Popis: | Background Our group has developed a new process for isolating and identifying novel cationic antimicrobial peptides from small amounts of biological samples. Previously, we identified several active antimicrobial peptides from 100 μl of plasma from Alligator mississippiensis. These peptides were found to have in vitro antimicrobial activity against Pseudomonas aeruginosa and Staphylococcus aureus. In this work, we further characterize three of the novel peptides discovered using this process: Apo5, Apo6, and A1P. Results We examined the activity of these peptides against multi-drug resistant strains and clinical isolates of common human pathogens. We investigated their structural characteristics using circular dichroism and tested for membrane disruption and DNA binding. These peptides were found to have strong in vitro activity against multi-drug resistant and clinically isolated strains of S. aureus, Escherichia coli, P. aeruginosa, and Acinetobacter baumannii. Apo5 and Apo6, peptides derived from alligator apolipoprotein C-1, depolarized the bacterial membrane. A1P, a peptide from the serpin proteinase inhibitor, did not permeabilize membranes. Performing circular dichroism analysis, Apo5 and Apo6 were found to be predominantly helical in SDS and TFE buffer, while A1P has significantly different structures in phosphate buffer, SDS, and TFE. None of these peptides were found to be hemolytic to sheep red blood cells or significantly cytotoxic up to 100 μg/ml after 24 h exposure. Conclusions Overall, we suggest that Apo5 and Apo6 have a different mode of action than A1P, and that all three peptides make promising candidates for the treatment of drug-resistant bacteria, such as A. baumannii. |
| Databáze: | OpenAIRE |
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