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Mapping the SARS-CoV-2–Host Protein–Protein Interactome by Affinity Purification Mass Spectrometry and Proximity-Dependent Biotin Labeling: A Rational and Straightforward Route to Discover Host-Directed Anti-SARS-CoV-2 Therapeutics

1
Department of Experimental and Clinical Medicine, University “Magna Græcia”, 88100 Catanzaro, Italy
2
Department of Health Sciences, University “Magna Græcia”, 88100 Catanzaro, Italy
3
Respiratory Medicine Unit, University “Magna Græcia”, 88100 Catanzaro, Italy
4
Department of Medical and Surgical Sciences, University “Magna Græcia”, 88100 Catanzaro, Italy
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2021, 22(2), 532; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22020532
Received: 17 December 2020 / Revised: 2 January 2021 / Accepted: 4 January 2021 / Published: 7 January 2021
(This article belongs to the Special Issue Molecular Research in Emerging Viruses 2020)
Protein–protein interactions (PPIs) are the vital engine of cellular machinery. After virus entry in host cells the global organization of the viral life cycle is strongly regulated by the formation of virus-host protein interactions. With the advent of high-throughput -omics platforms, the mirage to obtain a “high resolution” view of virus–host interactions has come true. In fact, the rapidly expanding approaches of mass spectrometry (MS)-based proteomics in the study of PPIs provide efficient tools to identify a significant number of potential drug targets. Generation of PPIs maps by affinity purification-MS and by the more recent proximity labeling-MS may help to uncover cellular processes hijacked and/or altered by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), providing promising therapeutic targets. The possibility to further validate putative key targets from high-confidence interactions between viral bait and host protein through follow-up MS-based multi-omics experiments offers an unprecedented opportunity in the drug discovery pipeline. In particular, drug repurposing, making use of already existing approved drugs directly targeting these identified and validated host interactors, might shorten the time and reduce the costs in comparison to the traditional drug discovery process. This route might be promising for finding effective antiviral therapeutic options providing a turning point in the fight against the coronavirus disease-2019 (COVID-19) outbreak. View Full-Text
Keywords: SARS-CoV-2; COVID-19; affinity-purification mass spectrometry; proximity-dependent biotin labeling (BioID); protein–protein interaction; proteomics; drug repurposing; virus; antiviral; emerging SARS-CoV-2; COVID-19; affinity-purification mass spectrometry; proximity-dependent biotin labeling (BioID); protein–protein interaction; proteomics; drug repurposing; virus; antiviral; emerging
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MDPI and ACS Style

Terracciano, R.; Preianò, M.; Fregola, A.; Pelaia, C.; Montalcini, T.; Savino, R. Mapping the SARS-CoV-2–Host Protein–Protein Interactome by Affinity Purification Mass Spectrometry and Proximity-Dependent Biotin Labeling: A Rational and Straightforward Route to Discover Host-Directed Anti-SARS-CoV-2 Therapeutics. Int. J. Mol. Sci. 2021, 22, 532. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22020532

AMA Style

Terracciano R, Preianò M, Fregola A, Pelaia C, Montalcini T, Savino R. Mapping the SARS-CoV-2–Host Protein–Protein Interactome by Affinity Purification Mass Spectrometry and Proximity-Dependent Biotin Labeling: A Rational and Straightforward Route to Discover Host-Directed Anti-SARS-CoV-2 Therapeutics. International Journal of Molecular Sciences. 2021; 22(2):532. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22020532

Chicago/Turabian Style

Terracciano, Rosa, Mariaimmacolata Preianò, Annalisa Fregola, Corrado Pelaia, Tiziana Montalcini, and Rocco Savino. 2021. "Mapping the SARS-CoV-2–Host Protein–Protein Interactome by Affinity Purification Mass Spectrometry and Proximity-Dependent Biotin Labeling: A Rational and Straightforward Route to Discover Host-Directed Anti-SARS-CoV-2 Therapeutics" International Journal of Molecular Sciences 22, no. 2: 532. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22020532

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