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Congresso Brasileiro de Microbiologia 2023
 		Resumo: 861-1

861-1

THE INTERACTION OF NATURAL PRODUCTS WITH THE HRSV M PROTEIN MAY PREVENT THE EFFICIENT BUDDING OF VIRAL PARTICLES

Autores:
Thainá dos Santos Rodrigues (UNESP - Institute of Biosciences, Letters and Exact Sciences ) ; Luana Seixas (UNESP - Institute of Biosciences, Letters and Exact Sciences ) ; Jéssica Maróstica de Sá (UNESP - Institute of Biosciences, Letters and Exact Sciences ) ; Isabella Otenio de Lourenço (UNESP - Institute of Biosciences, Letters and Exact Sciences ) ; Jefferson de Souza Busso (UNESP - Institute of Biosciences, Letters and Exact Sciences ) ; Luís Octávio Regasini (UNESP - Institute of Biosciences, Letters and Exact Sciences ) ; Ícaro Putinhon Caruso (UNESP - Institute of Biosciences, Letters and Exact Sciences ) ; Fátima Pereira de Souza (UNESP - Institute of Biosciences, Letters and Exact Sciences ) ; Marcelo Andres Fossey (UNESP - Institute of Biosciences, Letters and Exact Sciences )

Resumo:
The Respiratory Synccytial Virus (RSV) Matrix protein is responsable for a key step in the process for the virus assembles and buds through the plasma membrane, forming elongated membrane filaments through oligomerization and activity of the matrix protein M. This interaction between M and cellular receptors includes proteins involved, cytoskeketon regulation, membrane remodeling, and cellluar trafficking and the positive residual charged on the M protein domains may allow for its interaction with the negatively charged plasma membrane of pneumocytes, which likely serves to interacte with other viral and host proteins. In this context, natural produts have been important and can interact with important binding sites for proteins, preventing their action. The aim of this work was to verify the interaction of M protein and Coumarin, Resveratrol and Kaempferol by spectroscopic techniques. The M protein expression was proceeding in Escherichia coli and the protein was purified by affinity and molecular chromatography. The interaction assays were verified by spectroscopy titration. Results showed that Circular Dichroism analysis in the presence of the compound that the binding between them does not involve changes in the secundary structure of the protein. The fluorescence spectroscopy showed that Sterm-Volmer and the dissociation contant (Kb) is the order 104 M-1 for Coumarin, Resveratrol, and Kaempherol with similar values in the same order of interation. The thermodinamic analysis showed a hydrophobic binding for all ligands and the stoichiometry (n) of 1 ligand per protein. Biologically, these results of viral protein interaction with antioxidants enable us to interfere with potential effects on viral assembly or the formation of mature viruses, both of which are mediated by the M protein. Financial support: FAPESP, FINEP, CNPQ and Capes.

Palavras-chave:
 Matrix protein, Respiratory Synccytial Virus, Spectroscopic techniques, Natural products


Agência de fomento:
FAPESP, FINEP, CNPQ and Capes.