A BioID-Derived Proximity Interactome for SARS-CoV-2 Proteins.

Area of Science:

• Virology
• Molecular Biology
• Proteomics

Background:

• The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic poses significant global health and economic challenges.
• Understanding SARS-CoV-2 protein interactions within host cells is crucial for elucidating pathogenesis and developing effective antiviral treatments.

Purpose of the Study:

• To comprehensively map the SARS-CoV-2 virus-host interactome using proximity biotinylation (BioID).
• To identify cellular pathways influenced by SARS-CoV-2 proteins and discover potential therapeutic targets.

Main Methods:

• Global proteomic analysis was employed to assess the cellular impact of SARS-CoV-2 proteins.
• Proximity biotinylation (BioID) was utilized to map virus-host protein associations in human lung cancer cells.
• Functional enrichment analyses were performed on identified interactions.

Main Results:

• Previously known and novel cellular pathways associated with SARS-CoV-2 proteins were identified.
• A publicly accessible website was created to host proteomic data and facilitate further research.
• Sixty-six high-confidence virus-host interactions were confirmed by cross-referencing with prior studies.
• Potential therapeutic candidates were identified by screening interactors against the CLUE drug library.

Conclusions:

• This study provides a valuable resource for understanding SARS-CoV-2 biology at the molecular level.
• The identified host-viral interactions and potential drug targets can inform the development of new antiviral therapies for COVID-19.