Oral Presentation 28th Annual Lorne Proteomics Symposium 2023

Protein arginylation is regulated during SARS-CoV-2 infection (#42)

Giuseppe Palmisano 1
  1. Macquarie University, Sydney, NSW, Australia

Since 2019, the world has witnessed an unprecedented pandemic responsible for the death of more than 4 million people worldwide. A deep understanding of the molecular pathways dysregulated during SARS-CoV-2 infection can elucidate potential therapeutic targets and biomarkers. The N-terminal arginylation of proteins is characterized as an inducer of ubiquitination and proteasomal degradation by the N-end rule pathway. Our study focuses on the role of arginylation during SARS-CoV-2 infection. We studied the modulation of protein arginylation in SARS-CoV-2-infected Vero CCL-81 and Calu-3 cells. A combination of in vivo and in vitro public omics data reanalysis with immunoblotting and RTqPCR revealed an upregulation of arginyltransferase 1 (ATE1) and arginylated proteins. This regulation is specific to coronaviruses infections and the modulation of the N-end rule pathway differs between different types of infected cells. We also confirmed reduced viral load upon pharmacological and genetic inhibition of ATE1. These data show the importance of arginylation during SARS-CoV-2 infection.