Antiviral Activity of a Turbot ( Scophthalmus maximus ) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion
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 (Nkl...
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ftdoajarticles:oai:doaj.org/article:8188814ad1c94bce902d9d0e0b73290a 2023-05-15T18:15:44+02:00 Antiviral Activity of a Turbot ( Scophthalmus maximus ) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion Alberto Falco Regla María Medina-Gali José Antonio Poveda Melissa Bello-Perez Beatriz Novoa José Antonio Encinar 2019-02-01T00:00:00Z https://doi.org/10.3390/md17020087 https://doaj.org/article/8188814ad1c94bce902d9d0e0b73290a EN eng MDPI AG https://www.mdpi.com/1660-3397/17/2/87 https://doaj.org/toc/1660-3397 1660-3397 doi:10.3390/md17020087 https://doaj.org/article/8188814ad1c94bce902d9d0e0b73290a Marine Drugs, Vol 17, Iss 2, p 87 (2019) NK-lysin Nkl 71–100 phospholipid vesicles aggregation leakage phosphatidylserine antiviral viral fusion SVCV Biology (General) QH301-705.5 article 2019 ftdoajarticles https://doi.org/10.3390/md17020087 2022-12-30T20:00:55Z 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 (Nkl 71⁻100 ) 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 Nkl 71⁻100 with different glycerophospholipid vesicles. At acidic pH, Nkl 71⁻100 preferably interacts with phosphatidylserine (PS), disrupts PS membranes, and allows the content leakage from vesicles. Furthermore, Nkl 71⁻100 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, Nkl 71⁻100 is shown as a promising broad-spectrum antiviral candidate. Article in Journal/Newspaper Scophthalmus maximus Turbot Directory of Open Access Journals: DOAJ Articles Marine Drugs 17 2 87 |
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Open Polar |
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Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
NK-lysin Nkl 71–100 phospholipid vesicles aggregation leakage phosphatidylserine antiviral viral fusion SVCV Biology (General) QH301-705.5 |
spellingShingle |
NK-lysin Nkl 71–100 phospholipid vesicles aggregation leakage phosphatidylserine antiviral viral fusion SVCV Biology (General) QH301-705.5 Alberto Falco Regla María Medina-Gali José Antonio Poveda Melissa Bello-Perez Beatriz Novoa José Antonio Encinar Antiviral Activity of a Turbot ( Scophthalmus maximus ) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion |
topic_facet |
NK-lysin Nkl 71–100 phospholipid vesicles aggregation leakage phosphatidylserine antiviral viral fusion SVCV Biology (General) QH301-705.5 |
description |
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 (Nkl 71⁻100 ) 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 Nkl 71⁻100 with different glycerophospholipid vesicles. At acidic pH, Nkl 71⁻100 preferably interacts with phosphatidylserine (PS), disrupts PS membranes, and allows the content leakage from vesicles. Furthermore, Nkl 71⁻100 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, Nkl 71⁻100 is shown as a promising broad-spectrum antiviral candidate. |
format |
Article in Journal/Newspaper |
author |
Alberto Falco Regla María Medina-Gali José Antonio Poveda Melissa Bello-Perez Beatriz Novoa José Antonio Encinar |
author_facet |
Alberto Falco Regla María Medina-Gali José Antonio Poveda Melissa Bello-Perez Beatriz Novoa José Antonio Encinar |
author_sort |
Alberto Falco |
title |
Antiviral Activity of a Turbot ( Scophthalmus maximus ) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion |
title_short |
Antiviral Activity of a Turbot ( Scophthalmus maximus ) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion |
title_full |
Antiviral Activity of a Turbot ( Scophthalmus maximus ) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion |
title_fullStr |
Antiviral Activity of a Turbot ( Scophthalmus maximus ) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion |
title_full_unstemmed |
Antiviral Activity of a Turbot ( Scophthalmus maximus ) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion |
title_sort |
antiviral activity of a turbot ( scophthalmus maximus ) nk-lysin peptide by inhibition of low-ph virus-induced membrane fusion |
publisher |
MDPI AG |
publishDate |
2019 |
url |
https://doi.org/10.3390/md17020087 https://doaj.org/article/8188814ad1c94bce902d9d0e0b73290a |
genre |
Scophthalmus maximus Turbot |
genre_facet |
Scophthalmus maximus Turbot |
op_source |
Marine Drugs, Vol 17, Iss 2, p 87 (2019) |
op_relation |
https://www.mdpi.com/1660-3397/17/2/87 https://doaj.org/toc/1660-3397 1660-3397 doi:10.3390/md17020087 https://doaj.org/article/8188814ad1c94bce902d9d0e0b73290a |
op_doi |
https://doi.org/10.3390/md17020087 |
container_title |
Marine Drugs |
container_volume |
17 |
container_issue |
2 |
container_start_page |
87 |
_version_ |
1766188939705581568 |