BioID Combined with Mass Spectrometry to Study Herpesvirus Protein-Protein Interaction Networks

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 an...

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Bibliographic Details
Published inMethods in molecular biology (Clifton, N.J.) Vol. 2060; p. 327
Main Authors Cheerathodi, Mujeeb R, Meckes, Jr, David G
Format Journal Article
LanguageEnglish
Published United States 01.01.2020
Subjects
BioID
Biotin ligase
Affinity purification
Mass spectrometry
Proteomics
Herpesvirus
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Summary: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.
ISSN:1940-6029
DOI:10.1007/978-1-4939-9814-2_19