ArticleSTAR protocols2022
An antibody-based proximity labeling protocol to identify biotinylated interactors of SARS-CoV-2.
Article in STAR protocols, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Loss of ribosomal protein RPL22 restricts African swine fever virus replication by inducing PERK-dependent ER stress.Emerging microbes & infections · 2026Article
- A multiplex interactome of Ebola virus proteins reveals TM9SF2 as a cell-surface attachment factor that promotes viral entry.iMetaOmics · 2026Article
- The development of proximity labeling technology and its applications in mammals, plants, and microorganisms.Cell communication and signaling : CCS · 2023Review
- Mass Spectrometry-Based Proteomics Technologies to Define Endogenous Protein-Protein Interactions and Their Applications to Cancer and Viral Infectious Diseases.Mass spectrometry reviewsReview
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Authors and funding
8 authors.
Funding
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Abstract
Elucidating the molecular interactions between virus and host is fundamental to understanding the mechanism of viral pathogenesis. Here, we present a protocol to screen SARS-CoV-2 protein interactors using an antibody-based TurboID proximity labeling approach. This technique directly identifies biotinylated peptides labeled by the TurboID-tagged viral proteins. We describe the steps to prepare biotinylated peptide samples for mass spectrometry analysis and a stringent workflow to identify biotinylated high-confidence interactors of the virus by filtering out non-specific co-purified proteins. For complete details on the use and execution of this protocol, please refer to Zhang et al. (2022).
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