Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1038/s41598-021-88039-4 http://hdl.handle.net/11449/207935 |
Resumo: | Chikungunya virus (CHIKV) is the etiologic agent of Chikungunya fever, a globally spreading mosquito-borne disease. There is no approved antiviral or vaccine against CHIKV, highlighting an urgent need for novel therapies. In this context, snake venom proteins have demonstrated antiviral activity against several viruses, including arboviruses which are relevant to public health. In particular, the phospholipase A2CB (PLA2CB), a protein isolated from the venom of Crotalus durissus terrificus was previously shown to possess anti-inflammatory, antiparasitic, antibacterial and antiviral activities. In this study, we investigated the multiple effects of PLA2CB on the CHIKV replicative cycle in BHK-21 cells using CHIKV-nanoluc, a marker virus carrying nanoluciferase reporter. The results demonstrated that PLA2CB possess a strong anti-CHIKV activity with a selectivity index of 128. We identified that PLA2CB treatment protected cells against CHIKV infection, strongly impairing virus entry by reducing adsorption and post-attachment stages. Moreover, PLA2CB presented a modest yet significant activity towards post-entry stages of CHIKV replicative cycle. Molecular docking calculations indicated that PLA2CB may interact with CHIKV glycoproteins, mainly with E1 through hydrophobic interactions. In addition, infrared spectroscopy measurements indicated interactions of PLA2CB and CHIKV glycoproteins, corroborating with data from in silico analyses. Collectively, this data demonstrated the multiple antiviral effects of PLA2CB on the CHIKV replicative cycle, and suggest that PLA2CB interacts with CHIKV glycoproteins and that this interaction blocks binding of CHIKV virions to the host cells. |
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Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificusChikungunya virus (CHIKV) is the etiologic agent of Chikungunya fever, a globally spreading mosquito-borne disease. There is no approved antiviral or vaccine against CHIKV, highlighting an urgent need for novel therapies. In this context, snake venom proteins have demonstrated antiviral activity against several viruses, including arboviruses which are relevant to public health. In particular, the phospholipase A2CB (PLA2CB), a protein isolated from the venom of Crotalus durissus terrificus was previously shown to possess anti-inflammatory, antiparasitic, antibacterial and antiviral activities. In this study, we investigated the multiple effects of PLA2CB on the CHIKV replicative cycle in BHK-21 cells using CHIKV-nanoluc, a marker virus carrying nanoluciferase reporter. The results demonstrated that PLA2CB possess a strong anti-CHIKV activity with a selectivity index of 128. We identified that PLA2CB treatment protected cells against CHIKV infection, strongly impairing virus entry by reducing adsorption and post-attachment stages. Moreover, PLA2CB presented a modest yet significant activity towards post-entry stages of CHIKV replicative cycle. Molecular docking calculations indicated that PLA2CB may interact with CHIKV glycoproteins, mainly with E1 through hydrophobic interactions. In addition, infrared spectroscopy measurements indicated interactions of PLA2CB and CHIKV glycoproteins, corroborating with data from in silico analyses. Collectively, this data demonstrated the multiple antiviral effects of PLA2CB on the CHIKV replicative cycle, and suggest that PLA2CB interacts with CHIKV glycoproteins and that this interaction blocks binding of CHIKV virions to the host cells.Institute of Biomedical Science (ICBIM) Federal University of Uberlândia (UFU), Avenida Amazonas, 4C- Room 216, UmuaramaInstitute of Biosciences Humanities and Exact Sciences (Ibilce) São Paulo State University (Unesp), Campus São José do Rio PretoDepartment of Clinical Toxicological and Bromatological Analyses School of Pharmaceutical Sciences of Ribeirao Preto University of São Paulo (USP)Institute of Biotechnology Federal University of Uberlândia (UFU)Institute of Technology University of TartuFaculty of Biological Sciences and Astbury Centre for Structural Molecular Biology University of LeedsInstitute of Biosciences Humanities and Exact Sciences (Ibilce) São Paulo State University (Unesp), Campus São José do Rio PretoUniversidade Federal de Uberlândia (UFU)Universidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)University of TartuUniversity of LeedsSantos, Igor AndradeShimizu, Jacqueline Farinha [UNESP]de Oliveira, Débora MoraesMartins, Daniel Oliveira Silva [UNESP]Cardoso-Sousa, LéiaCintra, Adélia Cristina OliveiraAquino, Victor HugoSampaio, Suely VilelaNicolau-Junior, NilsonSabino-Silva, RobinsonMerits, AndresHarris, MarkJardim, Ana Carolina Gomes [UNESP]2021-06-25T11:03:27Z2021-06-25T11:03:27Z2021-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1038/s41598-021-88039-4Scientific Reports, v. 11, n. 1, 2021.2045-2322http://hdl.handle.net/11449/20793510.1038/s41598-021-88039-42-s2.0-85104693053Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengScientific Reportsinfo:eu-repo/semantics/openAccess2021-10-23T17:51:55Zoai:repositorio.unesp.br:11449/207935Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-23T17:51:55Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus |
title |
Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus |
spellingShingle |
Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus Santos, Igor Andrade |
title_short |
Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus |
title_full |
Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus |
title_fullStr |
Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus |
title_full_unstemmed |
Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus |
title_sort |
Chikungunya virus entry is strongly inhibited by phospholipase A2 isolated from the venom of Crotalus durissus terrificus |
author |
Santos, Igor Andrade |
author_facet |
Santos, Igor Andrade Shimizu, Jacqueline Farinha [UNESP] de Oliveira, Débora Moraes Martins, Daniel Oliveira Silva [UNESP] Cardoso-Sousa, Léia Cintra, Adélia Cristina Oliveira Aquino, Victor Hugo Sampaio, Suely Vilela Nicolau-Junior, Nilson Sabino-Silva, Robinson Merits, Andres Harris, Mark Jardim, Ana Carolina Gomes [UNESP] |
author_role |
author |
author2 |
Shimizu, Jacqueline Farinha [UNESP] de Oliveira, Débora Moraes Martins, Daniel Oliveira Silva [UNESP] Cardoso-Sousa, Léia Cintra, Adélia Cristina Oliveira Aquino, Victor Hugo Sampaio, Suely Vilela Nicolau-Junior, Nilson Sabino-Silva, Robinson Merits, Andres Harris, Mark Jardim, Ana Carolina Gomes [UNESP] |
author2_role |
author author author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Federal de Uberlândia (UFU) Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) University of Tartu University of Leeds |
dc.contributor.author.fl_str_mv |
Santos, Igor Andrade Shimizu, Jacqueline Farinha [UNESP] de Oliveira, Débora Moraes Martins, Daniel Oliveira Silva [UNESP] Cardoso-Sousa, Léia Cintra, Adélia Cristina Oliveira Aquino, Victor Hugo Sampaio, Suely Vilela Nicolau-Junior, Nilson Sabino-Silva, Robinson Merits, Andres Harris, Mark Jardim, Ana Carolina Gomes [UNESP] |
description |
Chikungunya virus (CHIKV) is the etiologic agent of Chikungunya fever, a globally spreading mosquito-borne disease. There is no approved antiviral or vaccine against CHIKV, highlighting an urgent need for novel therapies. In this context, snake venom proteins have demonstrated antiviral activity against several viruses, including arboviruses which are relevant to public health. In particular, the phospholipase A2CB (PLA2CB), a protein isolated from the venom of Crotalus durissus terrificus was previously shown to possess anti-inflammatory, antiparasitic, antibacterial and antiviral activities. In this study, we investigated the multiple effects of PLA2CB on the CHIKV replicative cycle in BHK-21 cells using CHIKV-nanoluc, a marker virus carrying nanoluciferase reporter. The results demonstrated that PLA2CB possess a strong anti-CHIKV activity with a selectivity index of 128. We identified that PLA2CB treatment protected cells against CHIKV infection, strongly impairing virus entry by reducing adsorption and post-attachment stages. Moreover, PLA2CB presented a modest yet significant activity towards post-entry stages of CHIKV replicative cycle. Molecular docking calculations indicated that PLA2CB may interact with CHIKV glycoproteins, mainly with E1 through hydrophobic interactions. In addition, infrared spectroscopy measurements indicated interactions of PLA2CB and CHIKV glycoproteins, corroborating with data from in silico analyses. Collectively, this data demonstrated the multiple antiviral effects of PLA2CB on the CHIKV replicative cycle, and suggest that PLA2CB interacts with CHIKV glycoproteins and that this interaction blocks binding of CHIKV virions to the host cells. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-06-25T11:03:27Z 2021-06-25T11:03:27Z 2021-12-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1038/s41598-021-88039-4 Scientific Reports, v. 11, n. 1, 2021. 2045-2322 http://hdl.handle.net/11449/207935 10.1038/s41598-021-88039-4 2-s2.0-85104693053 |
url |
http://dx.doi.org/10.1038/s41598-021-88039-4 http://hdl.handle.net/11449/207935 |
identifier_str_mv |
Scientific Reports, v. 11, n. 1, 2021. 2045-2322 10.1038/s41598-021-88039-4 2-s2.0-85104693053 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Scientific Reports |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
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1799964999159906304 |