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Mar. Drugs 2019, 17(2), 87; https://doi.org/10.3390/md17020087

Antiviral Activity of a Turbot (Scophthalmus maximus) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion

1
Instituto de Investigación, Desarrollo e Innovación en Biotecnología Sanitaria de Elche (IDiBE) and Instituto de Biología Molecular y Celular (IBMC), Miguel Hernández University (UMH); 03202 Elche Alicante, Spain
2
Instituto de Investigaciones Marinas (IIM), Consejo Superior de Investigaciones Científicas (CSIC), 36208 Vigo, Spain
*
Authors to whom correspondence should be addressed.
Received: 20 December 2018 / Revised: 10 January 2019 / Accepted: 23 January 2019 / Published: 1 February 2019
(This article belongs to the Special Issue Marine Small-Molecule Bioactive Agents and Therapeutic Targets)
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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. View Full-Text
Keywords: NK-lysin; Nkl71–100; phospholipid vesicles; aggregation; leakage; phosphatidylserine; antiviral; viral fusion; SVCV NK-lysin; Nkl71–100; phospholipid vesicles; aggregation; leakage; phosphatidylserine; antiviral; viral fusion; SVCV
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Falco, A.; Medina-Gali, R.M.; Poveda, J.A.; Bello-Perez, M.; Novoa, B.; Encinar, J.A. Antiviral Activity of a Turbot (Scophthalmus maximus) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion. Mar. Drugs 2019, 17, 87.

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