Broad-Spectrum Antiviral Activity of the Amphibian Antimicrobial Peptide Temporin L and Its Analogs
| Autor: | Carla Zannella, Annalisa Chianese, Luciana Palomba, Maria Elena Marcocci, Rosa Bellavita, Francesco Merlino, Paolo Grieco, Veronica Folliero, Anna De Filippis, Marialuisa Mangoni, Lucia Nencioni, Gianluigi Franci, Massimiliano Galdiero |
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| Přispěvatelé: | Zannella, Carla, Chianese, Annalisa, Palomba, Luciana, Marcocci, Maria Elena, Bellavita, Rosa, Merlino, Francesco, Grieco, Paolo, Folliero, Veronica, De Filippis, Anna, Mangoni, Marialuisa, Nencioni, Lucia, Franci, Gianluigi, Galdiero, Massimiliano, Zannella, C., Chianese, A., Palomba, L., Marcocci, M. E., Bellavita, R., Merlino, F., Grieco, P., Folliero, V., De Filippis, A., Mangoni, M., Nencioni, L., Franci, G., Galdiero, M. |
| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: |
antimicrobial peptide
Cell Survival amps temporin frog peptides Amphibian Protein Gram-Positive Bacteria Antiviral Agents Chlorocebus aethiop Catalysis Amphibian Proteins Inorganic Chemistry Amphibians antimicrobial peptides AMPs Antimicrobial peptides Antiviral activity Frog peptides HSV-1 SARS-CoV-2 Temporins Virus-host interaction Amino Acid Sequence Animals Antimicrobial Cationic Peptides Chlorocebus aethiops DNA Viruses Gram-Negative Bacteria Humans Lipids RNA Viruses Vero Cells Physical and Theoretical Chemistry temporins antiviral activity virus-host interaction hsv-1 sars-cov-2 Molecular Biology Spectroscopy AMP Antiviral Agent RNA Viruse Antimicrobial Cationic Peptide Animal Organic Chemistry General Medicine Amphibian Lipid Computer Science Applications frog peptide DNA Viruse Human |
| Zdroj: | International Journal of Molecular Sciences; Volume 23; Issue 4; Pages: 2060 |
| Popis: | The COVID-19 pandemic has evidenced the urgent need for the discovery of broad-spectrum antiviral therapies that could be deployed in the case of future emergence of novel viral threats, as well as to back up current therapeutic options in the case of drug resistance development. Most current antivirals are directed to inhibit specific viruses since these therapeutic molecules are designed to act on a specific viral target with the objective of interfering with a precise step in the replication cycle. Therefore, antimicrobial peptides (AMPs) have been identified as promising antiviral agents that could help to overcome this limitation and provide compounds able to act on more than a single viral family. We evaluated the antiviral activity of an amphibian peptide known for its strong antimicrobial activity against both Gram-positive and Gram-negative bacteria, namely Temporin L (TL). Previous studies have revealed that TL is endowed with widespread antimicrobial activity and possesses marked haemolytic activity. Therefore, we analyzed TL and a previously identified TL derivative (Pro3, DLeu9 TL, where glutamine at position 3 is replaced with proline, and the D-Leucine enantiomer is present at position 9) as well as its analogs, for their activity against a wide panel of viruses comprising enveloped, naked, DNA and RNA viruses. We report significant inhibition activity against herpesviruses, paramyxoviruses, influenza virus and coronaviruses, including SARS-CoV-2. Moreover, we further modified our best candidate by lipidation and demonstrated a highly reduced cytotoxicity with improved antiviral effect. Our results show a potent and selective antiviral activity of TL peptides, indicating that the novel lipidated temporin-based antiviral agents could prove to be useful additions to current drugs in combatting rising drug resistance and epidemic/pandemic emergencies. |
| Databáze: | OpenAIRE |
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