A BioID-derived proximity interactome for SARS-CoV-2 proteins

ABSTRACT: The novel coronavirus SARS-CoV-2 is responsible for the ongoing COVID-19 pandemic and has caused a major health and economic burden worldwide. Understanding how SARS-CoV-2 viral proteins behave in host cells can reveal underlying mechanisms of pathogenesis and assist in development of antiviral therapies. Here the cellular impact of expressing SARS-CoV-2 viral proteins was studied by global proteomic analysis and proximity biotinylation (BioID) was used to map the SARS-CoV-2 virus-host interactome in human lung cancer derived cells. Functional enrichment analyses revealed previously reported and unreported cellular pathways that are associated with SARS-CoV-2 proteins. We have also established a website to host the proteomic data to allow for public access and continued analysis of host-viral protein associations and whole-cell proteomes of cells expressing the viral-BioID fusion proteins. Furthermore, we identified 154 high-confidence interactions by comparing this study with previous reports, providing a strong foundation for future follow-up studies. Finally, we cross-referenced candidate interactors with the CLUE drug library to identify potential therapeutics for drug-repurposing efforts. Collectively, these studies provide a valuable resource to uncover novel SARS-CoV-2 biology and inform development of antivirals.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Alex Rosa Campos  

PROVIDER: MSV000088245 | MassIVE | Mon Oct 18 15:46:00 BST 2021

SECONDARY ACCESSION(S): PXD029207

REPOSITORIES: MassIVE