Interaction of Human Respiratory Syncytial Virus (HRSV) Matrix Protein with Resveratrol Shows Antiviral Effect

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorRodrigues, Thaina-
Autor(es): dc.creatorBusso, Jefferson de Souza-
Autor(es): dc.creatorDias, Raphael Vinicius Rodrigues-
Autor(es): dc.creatorOttenio Lourenço, Isabella-
Autor(es): dc.creatorde Sa, Jessica Maróstica-
Autor(es): dc.creatorCarvalho, Sidney Jurado de-
Autor(es): dc.creatorCaruso, Icaro Putinhon-
Autor(es): dc.creatorSouza, Fatima Pereira de-
Autor(es): dc.creatorFossey, Marcelo Andres-
Data de aceite: dc.date.accessioned2025-08-21T23:23:29Z-
Data de disponibilização: dc.date.available2025-08-21T23:23:29Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2024-11-30-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/ijms252312790-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/300829-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/300829-
Descrição: dc.descriptionThe respiratory syncytial virus (RSV) matrix protein plays key roles in the virus life cycle and is essential for budding, as it stimulates the optimal membrane curvature necessary for the emergence of viral particles. Resveratrol, a polyphenol (3,4′,5-trihydroxy-trans-stilbene) produced by plants, exhibits pharmacological effects, including anti-inflammatory and antiviral activities. In this study, resveratrol was tested in HEp-2 (Epidermoid carcinoma of the larynx cell) cells for its post-infection effects, and recombinant M protein was produced to characterize the biophysical mechanisms underlying this interaction. The CC50 (Cytotoxic concentration 50%) value for resveratrol was determined to be 297 μM over 48 h, and the results from the HEp-2 cell cultures demonstrated a viral inhibition of 42.7% in the presence of resveratrol, with an EC50 (Half maximal effective concentration) of 44.26 μM. This mechanism may occur through interaction with the M protein responsible for the budding of mature viral particles. Biophysical assays enabled us to characterize the interaction of the M/resveratrol complex as an entropically driven bond, guided by hydrophobic interactions at the dimerization interface of the M protein, which is essential for the stabilization and formation of the oligomers necessary for viral budding. These findings suggest that one of the targets for resveratrol binding is the M protein, indicating a potential site for blocking the progression of the infection.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionDepartment of Physics Institute of Biosciences Humanities and Exact Sciences São Paulo State University (UNESP), Rua Cristóvão Colombo, 2265, SP-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) São Paulo State University (UNESP), SP-
Descrição: dc.descriptionDepartment of Physics Institute of Biosciences Humanities and Exact Sciences São Paulo State University (UNESP), Rua Cristóvão Colombo, 2265, SP-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) São Paulo State University (UNESP), SP-
Descrição: dc.descriptionFAPESP: 2023/09642-7-
Descrição: dc.descriptionCNPq: 310898/2021-8-
Descrição: dc.descriptionCNPq: 317157/2023-0-
Descrição: dc.descriptionCAPES: AUXEP: 1548/2020-
Idioma: dc.languageen-
Relação: dc.relationInternational Journal of Molecular Sciences-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectand resveratrol-
Palavras-chave: dc.subjectM protein-
Palavras-chave: dc.subjectrespiratory syncytial virus-
Título: dc.titleInteraction of Human Respiratory Syncytial Virus (HRSV) Matrix Protein with Resveratrol Shows Antiviral Effect-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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