Biophysical and flavonoid-binding studies of the G protein ectodomain of group A human respiratory syncytial virus

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dc.contributor.authorMachado, Vitor Brassolatti [UNESP]
dc.contributor.authorMaróstica de Sá, Jéssica [UNESP]
dc.contributor.authorMiranda Prado, Ana Karla [UNESP]
dc.contributor.authorAlves de Toledo, Karina [UNESP]
dc.contributor.authorRegasini, Luis Octávio [UNESP]
dc.contributor.authorPereira de Souza, Fátima [UNESP]
dc.contributor.authorCaruso, Ícaro Putinhon [UNESP]
dc.contributor.authorFossey, Marcelo Andres [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2019-10-06T16:22:03Z
dc.date.available2019-10-06T16:22:03Z
dc.date.issued2019-03-01
dc.description.abstractThe human Respiratory Syncytial Virus (hRSV) is the major causative agent of lower respiratory tract diseases in infants, young children and elderly. The membrane protein G is embedded in the viral lipid envelope and plays an adhesion function of the virus to host cells. The present study reports the production of the group A hRSV recombinant G protein ectodomain (edG) and its characterization of secondary structure and thermal unfolding by circular dichroism (CD), as well as the binding investigation of flavonoids quercetin and morin to this protein by fluorescent quenching. CD data reveal that edG is composed mostly of β-structure and its melting temperature is of 325 K. Fluorescence quenching experiments of hRSV edG show that the dissociation constants for the flavonoids binding are micromolar and the binding affinity for the edG/quercetin complex is inversely dependent on rising temperature while is directly dependent for the edG/morin interaction. The thermodynamic parameters suggest that hydrophobic contacts are important for the edG/morin association while van der Waals forces and hydrogen bonds contribute to the stabilization of the edG/quercetin complex. Thus, data reported herein may contribute to the development of new treatment strategies that prevent the viral infection by hRSV.en
dc.description.affiliationInstituto de Biociências Letras e Ciências Exatas UNESP Department of Biology
dc.description.affiliationInstituto de Biociências Letras e Ciências Exatas UNESP Multiuser Center for Biomolecular Innovation Laboratory of Molecular Biology
dc.description.affiliationInstituto de Biociências Letras e Ciências Exatas UNESP Department of Physics
dc.description.affiliationFaculdade de Ciências e Letras UNESP Department of Biology Sciences
dc.description.affiliationInstituto de Biociências Letras e Ciências Exatas UNESP Department of Chemistry and Environmental Sciences
dc.description.affiliationUnespInstituto de Biociências Letras e Ciências Exatas UNESP Department of Biology
dc.description.affiliationUnespInstituto de Biociências Letras e Ciências Exatas UNESP Multiuser Center for Biomolecular Innovation Laboratory of Molecular Biology
dc.description.affiliationUnespInstituto de Biociências Letras e Ciências Exatas UNESP Department of Physics
dc.description.affiliationUnespFaculdade de Ciências e Letras UNESP Department of Biology Sciences
dc.description.affiliationUnespInstituto de Biociências Letras e Ciências Exatas UNESP Department of Chemistry and Environmental Sciences
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdFAPESP: 2015/09261-7
dc.description.sponsorshipIdFAPESP: 2016/01749-3
dc.identifierhttp://dx.doi.org/10.1016/j.heliyon.2019.e01394
dc.identifier.citationHeliyon, v. 5, n. 3, 2019.
dc.identifier.doi10.1016/j.heliyon.2019.e01394
dc.identifier.issn2405-8440
dc.identifier.lattes0992736452764550
dc.identifier.lattes4101562077663619
dc.identifier.scopus2-s2.0-85063356616
dc.identifier.urihttp://hdl.handle.net/11449/188876
dc.language.isoeng
dc.relation.ispartofHeliyon
dc.rights.accessRightsAcesso aberto
dc.sourceScopus
dc.subjectBiochemistry
dc.subjectBiophysics
dc.subjectMolecular biology
dc.titleBiophysical and flavonoid-binding studies of the G protein ectodomain of group A human respiratory syncytial virusen
dc.typeArtigo
unesp.author.lattes0992736452764550
unesp.author.lattes4101562077663619

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Artigos - Biologia - IBILCE
Artigos - Física - IBILCE
Artigos - Química e Ciências Ambientais - IBILCE