The Covid-19 pandemic is an ongoing global pandemic that has created an immense burden on health and economic systems globally, with 100s of millions of infections and millions of deaths worldwide. SARS-CoV-2 is an RNA coronavirus that encodes for many viral proteins that are responsible for further viral replication and sequestration of anti-viral host responses that culminate in Covid-19 infections and its related pathology. The interactions and mechanisms associated with interaction between the viral and host proteins during infections is not well understood. Understanding these mechanisms will aid in a better understanding infection of Covid-19 infections, which will ultimately lead to better treatments.
Here, scientists from multiple research organisations across the United States implemented a powerful proteomics method to map the SARS-CoV-2 virus–host interactions. Specifically, they use a technique known as BioID (where a biotin protein ligase is fused to the termini of viral proteins), which enables tagging of host proteins that interact with the virus proteins. These tagged viral proteins are then purified and analysed by liquid chromatography mass spectrometry to identify the host protein interactions. Using a Thermo Easy nano-LC system equipped with a 25 cm IonOpticks Aurora Series packed emitter column coupled to a Thermo Orbitrap Lumos, 26 of the 29 known viral proteins were studied, and their interactions with host cells investigated. Preliminary analysis of this work has revealed reported processes, as shared with other viral infections, and interestingly discovered many unreported cellular pathways. It is hoped that these new insights will aid in enhanced treatment of SARS-CoV-2 infections.
Covid-19 is a devastating infection that is not well understood, limiting treatment. Here, scientists demonstrate that SARS-COV-2 viral proteins interact with proteins of the host resulting in Covid-19 infection and disease. These findings can be used to limit viral-host interactions and better treat Covid-19 infections.
Read the full paper
A BioID-derived proximity interactome for SARS-CoV-2 proteins. bioRxiv : the preprint server for biology, 2021.09.17.460814. https://doi.org/10.1101/2021.09.17.460814. May, D. G., Martin-Sancho, L., Anschau, V., Liu, S., Chrisopulos, R. J., Scott, K. L., Halfmann, C. T., Peña, R. D., Pratt, D., Campos, A. R., & Roux, K. J.
Commentary by Muhammad Zenaidee, PhD
About the author
Muhammad holds a PhD in Chemistry from The University of New South Wales and has a strong background in the development of tools to enhance top-down and bottom-up proteomics. He utilises his knowledge and training to develop new proteomics tools and technologies for the proteomics community.
