Biophysical characterization of the matrix protein from the respiratory syncytial virus

• Grant number: 19/08739-1
• Support Opportunities: Scholarships in Brazil - Master
• Start date: August 01, 2019
• End date: February 28, 2021
• Field of knowledge: Health Sciences - Medicine
• Principal Investigator: Fátima Pereira de Souza
• Grantee: Giovana Cavenaghi Guimarães
• Host Institution: Instituto de Biociências, Letras e Ciências Exatas (IBILCE). Universidade Estadual Paulista (UNESP). Campus de São José do Rio Preto. São José do Rio Preto , SP, Brazil

Abstract

The human Respiratory Syncytial Virus (hRSV) is the main cause of infections in the inferior respiratory tract in children and elderly all over the world. From the Mononegaviralesorder and Orthopneumovirusgender the hRSV has its genome composed of RNA single-stranded negative sense with 10 genes which encode 11 proteins. The matrix protein is essential to viral cicle once it acts on the replication process interacting with the ribonucleoprotein complex (RNPs). Lately, the M protein interacts with the cellular cytoskeleton coordinating the RNPs transference to lipid rafts aiding the viral sprouting. Thus, for the success adressing and sprouting, M protein must interact not only with F, G, M2-1, N, and P protein but also with cellular mediators. The M protein may form dimers and oligomers that confer the viral particle a typical filamentous shape when close to the cell membrane. Therefore, understand the conformational changes that can occur in the protein at different conditions of pH, temperature, and salinity can may help to elucidate the effective mechanism of the M protein in the viral replication process. To achieve this objective is intended to obtain the recombinant M protein and perform circular dichroism, dynamic light scattering, and fluorescence spectroscopy experiments at different conditions of temperature, pH, and e ionic force. The results of the present study will make it possible to understand the stability, structure, and conformational equilibrium of the matrix protein, providing a better comprehension of the protein function and conformational structure during the viral replication. (AU)

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

CARUSO, ICARO P.; GUIMARAES, GIOVANA C.; MACHADO, VITOR B.; FOSSEY, MARCELO A.; WILLBOLD, DIETER; ALMEIDA, FABIO C. L.; SOUZA, FATIMA P.. Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs. Journal of Virology, v. 94, n. 23, DEC 2020. (10/18169-3, 19/08739-1, 18/08900-4, 09/53989-4)

Academic Publications

(References retrieved automatically from State of São Paulo Research Institutions)

GUIMARÃES, Giovana Cavenaghi. Biophysical-chemical characterization of the human respiratory syncytial virus matrix protein.. 2021. Master's Dissertation - Universidade Estadual Paulista (Unesp). Instituto de Biociências Letras e Ciências Exatas. São José do Rio Preto São José do Rio Preto.