Project description:SARS-CoV-2 is a positive single-stranded RNA virus which interacts at different stages with the host proteins of infected cells. These interactions are necessary for the host to recognize and block the replication of the virus. But, at the same time, the virus requires host proteins to translate, transcribe and replicate its genetic material. In order to identify the host proteins that interact with SARS-CoV-2 RNA, we adopted the RNA-protein interaction detection coupled to mass spectrometry (RaPID-MS) technology, which allows the purification and identification by MS-based proteomics of the proteins associated to a specific RNA of interest expressed in mammalian cells. In particular, we conducted the analysis on the more structured regions of SARS-CoV-2 RNA and retrieved several proteins specifically associated with each region. Overall, our data revealed a list of proteins associated to SARS-CoV-2 RNA that will be further characterized to understand their role in SARS-CoV-2 infection and viral replication.
Project description:During Drosophila oogenesis, the localization and translational regulation of maternal transcripts relies on RNA-binding proteins (RBPs). Many of these RBPs localize several mRNAs and may have additional direct interaction partners to regulate their functions. Using immunoprecipitation from whole Drosophila ovaries coupled to mass spectrometry, we examined protein-protein associations of 6 GFP-tagged RBPs expressed at physiological levels. Analysis of the interaction network and further validation in human cells allowed us to identify 26 previously unknown associations, besides recovering several well characterized interactions.