Glycosylation of SARS-CoV-2 to identify the structural characteristics of COVID-19

• Grant number: 21/00507-4
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• Start date: February 01, 2021
• End date: January 31, 2023
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal Investigator: Giuseppe Palmisano
• Grantee: Vinícius de Morais Gomes
• Host Institution: Instituto de Ciências Biomédicas (ICB). Universidade de São Paulo (USP). São Paulo , SP, Brazil
• Associated research grant: 20/04923-0 - SARS-CoV-2 glycosylation: a blueprint structural insight for understanding COVID-19 pathogenesis, AP.R

Abstract

COVID-19 is a human respiratory syndrome caused by SARS-CoV-2 virus infection that has a high rate of infection and mortality. Viruses modulate the host's machinery by altering cellular mechanisms that favor its replication. One of the mechanisms exploited by viruses is protein glycosylation that occurs in the endoplasmic reticulum (ER) and Golgi complex. When ER function is impaired, there is an accumulation of unfolded proteins leading to ER stress. To maintain homeostasis, the cells trigger an adaptive signaling mechanism called Unfolded Proetin Response (UPR), which helps cells deal with stress, but in severe conditions, this process activates apoptosis. UPR forms a barrier to intracellular pathogens, such as viruses, preventing their survival. Therefore, it is necessary to study the cellular functioning of the processes of protein glycosylation and UPR in order to develop a therapy for the treatment of COVID-19. (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)

MULE, SIMON NGAO; GOMES, VINICIUS DE MORAIS; WAILEMANN, ROSANGELA A. M.; MACEDO-DA-SILVA, JANAINA; ROSA-FERNANDES, LIVIA; LARSEN, MARTIN R.; LABRIOLA, LETICIA; PALMISANO, GIUSEPPE. HSPB1 influences mitochondrial respiration in ER-stressed beta cells. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v. 1869, n. 9, SEP 2021. (17/04032-5, 14/02745-6, 17/03618-6, 18/18257-1, 16/04676-7, 20/04923-0, 16/14845-0, 13/07937-8, 18/15549-1, 21/00507-4)