PUBLICATION
Antiviral Activity of a Turbot (Scophthalmus maximus) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion
- Authors
- Falco, A., Medina-Gali, R.M., Poveda, J.A., Bello-Perez, M., Novoa, B., Encinar, J.A.
- ID
- ZDB-PUB-190206-1
- Date
- 2019
- Source
- Marine drugs 17(2): (Journal)
- Registered Authors
- Novoa, Beatriz
- Keywords
- NK-lysin, Nkl71–100, SVCV, aggregation, antiviral, leakage, phosphatidylserine, phospholipid vesicles, viral fusion
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Antiviral Agents/chemistry
- Antiviral Agents/pharmacology*
- Cell Line
- Cyprinidae
- Fish Diseases/drug therapy
- Fish Diseases/virology
- Flatfishes*
- Hydrogen-Ion Concentration
- Peptide Fragments/chemistry
- Peptide Fragments/pharmacology*
- Phospholipids/chemistry
- Phospholipids/pharmacology
- Proteolipids/chemistry*
- Proteolipids/pharmacology*
- Rhabdoviridae/drug effects*
- Rhabdoviridae/physiology
- Viremia/drug therapy
- Viremia/virology
- Virus Internalization/drug effects*
- Virus Replication/drug effects
- PubMed
- 30717094 Full text @ Mar. Drugs
Citation
Falco, A., Medina-Gali, R.M., Poveda, J.A., Bello-Perez, M., Novoa, B., Encinar, J.A. (2019) Antiviral Activity of a Turbot (Scophthalmus maximus) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion. Marine drugs. 17(2).
Abstract
Global health is under attack by increasingly-frequent pandemics of viral origin. Antimicrobial peptides are a valuable tool to combat pathogenic microorganisms. Previous studies from our group have shown that the membrane-lytic region of turbot (Scophthalmus maximus) NK-lysine short peptide (Nkl71⁻100) exerts an anti-protozoal activity, probably due to membrane rupture. In addition, NK-lysine protein is highly expressed in zebrafish in response to viral infections. In this work several biophysical methods, such as vesicle aggregation, leakage and fluorescence anisotropy, are employed to investigate the interaction of Nkl71⁻100 with different glycerophospholipid vesicles. At acidic pH, Nkl71⁻100 preferably interacts with phosphatidylserine (PS), disrupts PS membranes, and allows the content leakage from vesicles. Furthermore, Nkl71⁻100 exerts strong antiviral activity against spring viremia of carp virus (SVCV) by inhibiting not only the binding of viral particles to host cells, but also the fusion of virus and cell membranes, which requires a low pH context. Such antiviral activity seems to be related to the important role that PS plays in these steps of the replication cycle of SVCV, a feature that is shared by other families of virus-comprising members with health and veterinary relevance. Consequently, Nkl71⁻100 is shown as a promising broad-spectrum antiviral candidate.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping