Quantitative, TMT-based proteomics and phosphoproteomics analysis of SARS-COV-2 infected cells.

ABSTRACT: Host kinases play essential roles in the host cell cycle, innate immune signaling, the stress response to viral infection, and inflammation. Previous work has demonstrated coronaviruses specifically target kinase cascades to subvert host cell responses to infection and rely upon host kinase activity to phosphorylate viral proteins to enhance replication. Given the number of kinase inhibitors that are already FDA approved to treat cancers, fibrosis, and other human disease, they represent an attractive class of compounds to repurpose for host targeted therapies against emerging coronavirus infections. To further understand the host kinome response to betacoronavirus infection we employed multiplex inhibitory bead mass spectrometry (MIB-MS) following MERS-CoV and SARS-CoV-2 infection of human lung epithelial cell lines. To determine signaling pathways altered over the SARS-CoV-2 time-course, global quantitative phosphoproteomic and proteomic analysis of SARS-CoV-2 infected A549-hACE2 was performed on paired cell lysates (n=3) from the MIB-MS analysis. This PRIDE Submission contains the proteome and phosphoproteome data. The MIB-MS data were uploaded as a separate PRIDE Submission. Over 7,200 proteins and 14,300 phosphosites were quantified over the 24 hr infection time course. Further analysis of the phosphoproteome indicated activation of MAPK, PI3K, and mTOR signaling.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

DISEASE(S): Covid-19

SUBMITTER: Angie Mordant  

LAB HEAD: Ralph Baric

PROVIDER: PXD040897 | Pride | 2023-08-01

REPOSITORIES: Pride