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 (Nkl71–...
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Multidisciplinary Digital Publishing Institute
2019
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Online Access: | http://hdl.handle.net/10261/177043 https://doi.org/10.3390/md17020087 https://doi.org/10.13039/501100003329 https://doi.org/10.13039/501100003359 https://doi.org/10.13039/501100003339 https://doi.org/10.13039/501100010801 |
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ftcsic:oai:digital.csic.es:10261/177043 2024-02-11T10:08:26+01:00 Antiviral Activity of a Turbot (Scophthalmus maximus) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion Falcó, Alberto Medina-Gali, Regla María Poveda, José Antonio Bello Pérez, Melissa Novoa, Beatriz Encinar, José Antonio Consejo Superior de Investigaciones Científicas (España) Ministerio de Economía y Competitividad (España) Xunta de Galicia Generalitat Valenciana 2019-02-01 http://hdl.handle.net/10261/177043 https://doi.org/10.3390/md17020087 https://doi.org/10.13039/501100003329 https://doi.org/10.13039/501100003359 https://doi.org/10.13039/501100003339 https://doi.org/10.13039/501100010801 unknown Multidisciplinary Digital Publishing Institute #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2014-51773-C3-1-R info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2015-67995-C3-1-R info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2017-82851-C3-1-R Publisher's version http://dx.doi.org/10.3390/md17020087 Sí Marine Drugs 17(2): 87 (2019) 1660-3397 http://hdl.handle.net/10261/177043 doi:10.3390/md17020087 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100003359 http://dx.doi.org/10.13039/501100003339 http://dx.doi.org/10.13039/501100010801 30717094 open NK-lysin Nkl71–100 Phospholipid vesicles Aggregation Leakage Phosphatidylserine Antiviral Viral fusion SVCV artículo http://purl.org/coar/resource_type/c_6501 2019 ftcsic https://doi.org/10.3390/md1702008710.13039/50110000332910.13039/50110000335910.13039/50110000333910.13039/501100010801 2024-01-16T10:36:43Z 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. This research was funded by the Spanish Ministry of Science and Innovation, grant numbers AGL2014-51773-C3-1-R, AGL2015-67995-C3-1-R, BIO2017-82851-C3-1-R and PIE 201230E057; Xunta de Galicia (GAIN), grant number IN607B 2016/12, and Generalitat Valenciana, grant numbers ACIF/2016/207 and PROMETEO/2016/006. We acknowledge support by the CSIC Open Access Publication Initiative through its Unit of Information Resources for Research (URICI) Peer reviewed Article in Journal/Newspaper Scophthalmus maximus Turbot Digital.CSIC (Spanish National Research Council) Marine Drugs 17 2 87 |
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Open Polar |
collection |
Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
unknown |
topic |
NK-lysin Nkl71–100 Phospholipid vesicles Aggregation Leakage Phosphatidylserine Antiviral Viral fusion SVCV |
spellingShingle |
NK-lysin Nkl71–100 Phospholipid vesicles Aggregation Leakage Phosphatidylserine Antiviral Viral fusion SVCV Falcó, Alberto Medina-Gali, Regla María Poveda, José Antonio Bello Pérez, Melissa Novoa, Beatriz Encinar, José Antonio Antiviral Activity of a Turbot (Scophthalmus maximus) NK-Lysin Peptide by Inhibition of Low-pH Virus-Induced Membrane Fusion |
topic_facet |
NK-lysin Nkl71–100 Phospholipid vesicles Aggregation Leakage Phosphatidylserine Antiviral Viral fusion SVCV |
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 (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. This research was funded by the Spanish Ministry of Science and Innovation, grant numbers AGL2014-51773-C3-1-R, AGL2015-67995-C3-1-R, BIO2017-82851-C3-1-R and PIE 201230E057; Xunta de Galicia (GAIN), grant number IN607B 2016/12, and Generalitat Valenciana, grant numbers ACIF/2016/207 and PROMETEO/2016/006. We acknowledge support by the CSIC Open Access Publication Initiative through its Unit of Information Resources for Research (URICI) Peer reviewed |
author2 |
Consejo Superior de Investigaciones Científicas (España) Ministerio de Economía y Competitividad (España) Xunta de Galicia Generalitat Valenciana |
format |
Article in Journal/Newspaper |
author |
Falcó, Alberto Medina-Gali, Regla María Poveda, José Antonio Bello Pérez, Melissa Novoa, Beatriz Encinar, José Antonio |
author_facet |
Falcó, Alberto Medina-Gali, Regla María Poveda, José Antonio Bello Pérez, Melissa Novoa, Beatriz Encinar, José Antonio |
author_sort |
Falcó, Alberto |
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 |
Multidisciplinary Digital Publishing Institute |
publishDate |
2019 |
url |
http://hdl.handle.net/10261/177043 https://doi.org/10.3390/md17020087 https://doi.org/10.13039/501100003329 https://doi.org/10.13039/501100003359 https://doi.org/10.13039/501100003339 https://doi.org/10.13039/501100010801 |
genre |
Scophthalmus maximus Turbot |
genre_facet |
Scophthalmus maximus Turbot |
op_relation |
#PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2014-51773-C3-1-R info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2015-67995-C3-1-R info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2017-82851-C3-1-R Publisher's version http://dx.doi.org/10.3390/md17020087 Sí Marine Drugs 17(2): 87 (2019) 1660-3397 http://hdl.handle.net/10261/177043 doi:10.3390/md17020087 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100003359 http://dx.doi.org/10.13039/501100003339 http://dx.doi.org/10.13039/501100010801 30717094 |
op_rights |
open |
op_doi |
https://doi.org/10.3390/md1702008710.13039/50110000332910.13039/50110000335910.13039/50110000333910.13039/501100010801 |
container_title |
Marine Drugs |
container_volume |
17 |
container_issue |
2 |
container_start_page |
87 |
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1790607773888675840 |