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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

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

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Autor(es):
Machado, Vitor Brassolatti [1, 2] ; de Sa, Jessica Marostica [1, 3] ; Miranda Prado, Ana Karla [1, 3] ; de Toledo, Karina Alves [4] ; Regasini, Luis Octavio [5] ; de Souza, Fatima Pereira [1, 3] ; Caruso, Icaro Putinhon [1, 3] ; Fossey, Marcelo Andres [1, 3]
Número total de Autores: 8
Afiliação do(s) autor(es):
[1] UNESP, Inst Biociencias Letras & Ciencias Exatas, Lab Mol Biol, Multiuser Ctr Bimol Innovat, Sao Jose Do Rio Preto, SP - Brazil
[2] UNESP, Inst Biociencias Letras & Ciencias Exatas, Dept Biol, Sao Jose Do Rio Preto, SP - Brazil
[3] UNESP, Dept Phys, Inst Biociencias Letras & Ciencias Exatas, Sao Jose Do Rio Preto, SP - Brazil
[4] UNESP, Dept Biol Sci, Fac Ciencias & Letras, Assis, SP - Brazil
[5] UNESP, Inst Biociencias Letras & Ciencias Exatas, Dept Chem & Environm Sci, Sao Jose Do Rio Preto, SP - Brazil
Número total de Afiliações: 5
Tipo de documento: Artigo Científico
Fonte: HELIYON; v. 5, n. 3 MAR 2019.
Citações Web of Science: 0
Resumo

The 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 beta-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. (AU)

Processo FAPESP: 16/01749-3 - Busca de alvos antivirais contra o vírus sincicial respiratório humano, utilizando as proteínas de superfícies como sítio de bloqueio
Beneficiário:Marcelo Andrés Fossey
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 15/09261-7 - Estudo da interação da proteína g do vírus sincicial respiratório humano com flavonóides para desenho de antivirais
Beneficiário:Vitor Brassolatti Machado
Linha de fomento: Bolsas no Brasil - Iniciação Científica