Abstract
Herpes viruses are important human pathogens that cause a wide range of diseases from skin lesions to malignancies. Protein interactions drive many cellular events and mediate a number of biochemical pathways leading to different physiological outcomes. Protein interactions between viral proteins and host proteins play significant roles in viral entry, replication and suppression of host-immune responses. Therefore, the study of virus–host interactions promises significant advancement in designing therapeutics to control infection and disease. Various approaches are employed in the field to study and identify protein interactions that combine affinity purification along with different detection methods. Advancements in protein purification and high-throughput detection methods have resulted in an unprecedented level of discovery. Here we detail the use of proximity dependent biotinylation (BioID) as a means of affinity purification coupled with the use of LC-MS/MS for the detection and identification of protein–protein interaction networks.
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Acknowledgments
Special thanks to Mark Rider initiating the use of the BioID method in the lab. The method described in this chapter was developed with the support of grants from the National Institutes of Health (CA204621 and CA188941) awarded to D.G.M.
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Cheerathodi, M.R., Meckes, D.G. (2020). BioID Combined with Mass Spectrometry to Study Herpesvirus Protein–Protein Interaction Networks. In: Diefenbach, R., Fraefel, C. (eds) Herpes Simplex Virus . Methods in Molecular Biology, vol 2060. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9814-2_19
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