Characterization of the relationship between SARS-CoV-2 NSP9 and host interactors

• Grant number: 23/04255-5
• Support Opportunities: Scholarships abroad - Research Internship - Doctorate
• Start date: August 30, 2023
• End date: August 29, 2024
• Field of knowledge: Biological Sciences - Biochemistry - Molecular Biology
• Principal Investigator: Fernando Moreira Simabuco
• Grantee: Luiz Guilherme Salvino da Silva
• Supervisor: Alexander Khromykh
• Host Institution: Faculdade de Ciências Aplicadas (FCA). Universidade Estadual de Campinas (UNICAMP). Limeira , SP, Brazil
• Institution abroad: University of Queensland, Brisbane (UQ), Australia
• Associated to the scholarship: 20/09527-5 - SARS-CoV-2 Nsp9 protein in oxidative stress: nutraceuticals as a therapeutic approach, BP.DR

Abstract

A new outbreak of lung disease caused by a new coronavirus emerged in Wuhan (capital of Hubei Province in China) in December 2019 and, since spread to different parts of the world which, has led the World Health Organization to confirm the outbreak as a pandemic on March 11, 2020, naming the new virus SARS-CoV-2. NSP9, the non-structural protein (NSP) 9 of SARS-CoV-2, directly participates in the viral infectious cycle and has already proved to be essential for its replication, participating in capping and priming nascent viral RNAs. Human proteins that interact with NSP9 were recently identified by us, suggesting possible functions not previously attributed to NSP9, however, there is no clear information either on how these proteins interact or where in the protein they could interact with each other. This project aims to better understand NSP9 host interactions by using replicons. We also propose the use of drug libraries to evaluate an inhibitory drug against SARS-CoV-2 and targeting NSP9-host proteins interaction, also studying NSP9 already known functions. Therefore, we hypothesize that the interactions made by NSP9 already validated by us can play an important role in viral replication and/or maintenance in the host cell and that specific mutations or drug competition on the sites of interaction with those proteins may reflect a virus inhibition and a better understanding of the viral interacting network. (AU)