Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper

Secreted phospholipase A2 (sPLA2) molecules are small, calcium-dependent enzymes involved in many biological processes. Viperid venoms possess gIIA sPLA2s and sPLA2-like proteins, both having homology to human gIIA sPLA2, an innate immunity enzyme. We evaluated the antiviral action of Mt–I (catalyti...

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Detalhes bibliográficos
Autores: Brenes Porras, Hebleen, Loría Masís, Gilbert David, Lomonte, Bruno
Formato: artículo
Fecha de publicación:2020
País:Costa Rica
Recursos:Universidad de Costa Rica
Repositorio:Kérwá
Idioma:inglés
OAI Identifier:oai:kerwa.ucr.ac.cr:10669/82939
Acesso em linha:https://www.sciencedirect.com/science/article/abs/pii/S1045105619301332?via%3Dihub
https://hdl.handle.net/10669/82939
Access Level:acceso abierto
Palavra-chave:Phospholipase A2
Virucidal
Flaviviridae
Enveloped virus
Dengue
Snake venom
id CR_85aba06f33a4c170ea4d263175a07dbf
oai_identifier_str oai:kerwa.ucr.ac.cr:10669/82939
network_acronym_str CR
network_name_str Costa Rica
repository_id_str
dc.title.es_ES.fl_str_mv Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper
title Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper
spellingShingle Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper
Brenes Porras, Hebleen
Phospholipase A2
Virucidal
Flaviviridae
Enveloped virus
Dengue
Snake venom
title_short Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper
title_full Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper
title_fullStr Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper
title_full_unstemmed Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper
title_sort Potent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asper
dc.creator.none.fl_str_mv Brenes Porras, Hebleen
Loría Masís, Gilbert David
Lomonte, Bruno
author Brenes Porras, Hebleen
author_facet Brenes Porras, Hebleen
Loría Masís, Gilbert David
Lomonte, Bruno
author_role author
author2 Loría Masís, Gilbert David
Lomonte, Bruno
author2_role author
author
dc.subject.es_ES.fl_str_mv Phospholipase A2
Virucidal
Flaviviridae
Enveloped virus
Dengue
Snake venom
topic Phospholipase A2
Virucidal
Flaviviridae
Enveloped virus
Dengue
Snake venom
description Secreted phospholipase A2 (sPLA2) molecules are small, calcium-dependent enzymes involved in many biological processes. Viperid venoms possess gIIA sPLA2s and sPLA2-like proteins, both having homology to human gIIA sPLA2, an innate immunity enzyme. We evaluated the antiviral action of Mt–I (catalytically-active sPLA2) and Mt-II (catalytically-inactive variant) isolated from the venom of Bothrops asper, against a diverse group of viruses. Yellow Fever and Dengue (enveloped) viruses were highly susceptible to inactivation by the snake proteins, in contrast to Sabin (non-enveloped; Polio vaccine strain), and Influenza A, Herpes simplex 1 and 2, and Vesicular Stomatitis (enveloped) viruses. Titration of the antiviral effect against Dengue virus revealed Mt–I to be highly potent (IC50 0.5–2 ng/mL), whereas Mt-II was 1000-fold weaker. This large difference suggested a requirement for PLA2 activity, which was confirmed by chemical inactivation of Mt–I. A synthetic peptide representing the membrane-disrupting region of Mt-II, previously shown to have bactericidal effect, lacked antiviral action, suggesting that the weak virucidal effect observed for Mt-II is likely caused by contamination with traces of Mt–I. On the other hand, Mt–I was demonstrated to act by a direct virucidal mechanism prior to infection, and not by an independent effect on host cells, either pretreated, or exposed to Mt–I after virus infection. Interestingly, DENV2 propagated in mosquito cells was much more sensitive to the action of Mt–I, compared to human cell-propagated virus. Therefore, differences in envelope membrane composition may be crucially involved in the observed virucidal action of PLA2 enzymes.
publishDate 2020
dc.date.issued.none.fl_str_mv 2020
dc.date.accessioned.none.fl_str_mv 2021-03-02T20:29:33Z
dc.date.available.none.fl_str_mv 2021-03-02T20:29:33Z
dc.type.none.fl_str_mv artículo original
http://purl.org/coar/resource_type/c_2df8fbb1
info:eu-repo/semantics/article
format article
dc.identifier.citation.none.fl_str_mv https://www.sciencedirect.com/science/article/abs/pii/S1045105619301332?via%3Dihub
dc.identifier.issn.none.fl_str_mv 1045-1056
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/10669/82939
dc.identifier.doi.none.fl_str_mv 10.1016/j.biologicals.2019.12.002
dc.identifier.codproyecto.none.fl_str_mv 803-B8-115
url https://www.sciencedirect.com/science/article/abs/pii/S1045105619301332?via%3Dihub
https://hdl.handle.net/10669/82939
identifier_str_mv 1045-1056
10.1016/j.biologicals.2019.12.002
803-B8-115
dc.language.iso.es_ES.fl_str_mv eng
language eng
dc.rights.es_ES.fl_str_mv acceso abierto
dc.rights.none.fl_str_mv http://purl.org/coar/access_right/c_abf2
info:eu-repo/semantics/openAccess
rights_invalid_str_mv acceso abierto
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.source.es_ES.fl_str_mv Biologicals, vol.63, pp.48-52
dc.source.none.fl_str_mv reponame:Kérwá
instname:Universidad de Costa Rica
instacron:UCR
instname_str Universidad de Costa Rica
instacron_str UCR
institution UCR
reponame_str Kérwá
collection Kérwá
bitstream.url.fl_str_mv https://www.kerwa.ucr.ac.cr/bitstreams/1b076258-9306-4cd1-8197-a706dd51e371/download
bitstream.checksum.fl_str_mv bc4aed01f809e5c64e810e000d6a48b8
bitstream.checksumAlgorithm.fl_str_mv MD5
repository.name.fl_str_mv Kérwá - Universidad de Costa Rica
repository.mail.fl_str_mv meilyn.garro@ucr.ac.cr
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spelling Brenes Porras, Hebleencec3d310-c7e1-47a2-abe6-a352092924ebLoría Masís, Gilbert Davidf1d1bd13-72b6-47a1-a3cc-aa6b1dc37fdd600Lomonte, Bruno581484ad-aaa8-46b1-bc0e-f380d895640c6002021-03-02T20:29:33Z2021-03-02T20:29:33Z2020https://www.sciencedirect.com/science/article/abs/pii/S1045105619301332?via%3Dihub1045-1056https://hdl.handle.net/10669/8293910.1016/j.biologicals.2019.12.002803-B8-115Secreted phospholipase A2 (sPLA2) molecules are small, calcium-dependent enzymes involved in many biological processes. Viperid venoms possess gIIA sPLA2s and sPLA2-like proteins, both having homology to human gIIA sPLA2, an innate immunity enzyme. We evaluated the antiviral action of Mt–I (catalytically-active sPLA2) and Mt-II (catalytically-inactive variant) isolated from the venom of Bothrops asper, against a diverse group of viruses. Yellow Fever and Dengue (enveloped) viruses were highly susceptible to inactivation by the snake proteins, in contrast to Sabin (non-enveloped; Polio vaccine strain), and Influenza A, Herpes simplex 1 and 2, and Vesicular Stomatitis (enveloped) viruses. Titration of the antiviral effect against Dengue virus revealed Mt–I to be highly potent (IC50 0.5–2 ng/mL), whereas Mt-II was 1000-fold weaker. This large difference suggested a requirement for PLA2 activity, which was confirmed by chemical inactivation of Mt–I. A synthetic peptide representing the membrane-disrupting region of Mt-II, previously shown to have bactericidal effect, lacked antiviral action, suggesting that the weak virucidal effect observed for Mt-II is likely caused by contamination with traces of Mt–I. On the other hand, Mt–I was demonstrated to act by a direct virucidal mechanism prior to infection, and not by an independent effect on host cells, either pretreated, or exposed to Mt–I after virus infection. Interestingly, DENV2 propagated in mosquito cells was much more sensitive to the action of Mt–I, compared to human cell-propagated virus. Therefore, differences in envelope membrane composition may be crucially involved in the observed virucidal action of PLA2 enzymes.Universidad de Costa Rica/[803-B8-115]/UCR/Costa RicaUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)engacceso abiertohttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessBiologicals, vol.63, pp.48-52reponame:Kérwáinstname:Universidad de Costa Ricainstacron:UCRPhospholipase A2VirucidalFlaviviridaeEnveloped virusDengueSnake venomPotent virucidal activity against Flaviviridae of a group IIA phospholipase A2 isolated from the venom of Bothrops asperartículo originalhttp://purl.org/coar/resource_type/c_2df8fbb1info:eu-repo/semantics/articleLICENSElicense.txtlicense.txttext/plain; charset=utf-82901https://www.kerwa.ucr.ac.cr/bitstreams/1b076258-9306-4cd1-8197-a706dd51e371/downloadbc4aed01f809e5c64e810e000d6a48b8MD5110669/829392024-05-22 08:23:49.104metadata.onlyoai:kerwa.ucr.ac.cr:10669/82939https://www.kerwa.ucr.ac.crInstitucionalhttp://www.kerwa.ucr.ac.crUniversidadhttp://www.ucr.ac.crhttps://kerwa.ucr.ac.cr/oai/requestmeilyn.garro@ucr.ac.crCosta RicaNo aplicaNo aplicaNo aplicaopendoar:18712025-03-29T18:00:49Kérwá - 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