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Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins
Published on: August 31, 2017
BioID Combined with Mass Spectrometry to Study Herpesvirus Protein-Protein Interaction Networks
Mujeeb R Cheerathodi1, David G Meckes2
1Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL, USA.
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.
Insights
Researchers explored herpes virus and human protein interactions using proximity dependent biotinylation (BioID) and LC-MS/MS. This method aids in identifying viral protein interactions for developing new antiviral therapies.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Herpesviruses are significant human pathogens causing diverse diseases, including skin lesions and cancers.
- Viral protein interactions with host proteins are crucial for viral entry, replication, and immune evasion.
- Understanding these virus-host interactions is key to developing effective antiviral therapies.
Purpose of the Study:
- To detail the application of proximity dependent biotinylation (BioID) for studying virus-host protein interactions.
- To identify protein-protein interaction networks involved in herpesvirus infections.
- To advance the development of novel therapeutic strategies against herpesvirus diseases.
Main Methods:
- Utilized proximity dependent biotinylation (BioID) for affinity purification of interacting proteins.
- Employed liquid chromatography-tandem mass spectrometry (LC-MS/MS) for high-throughput detection and identification of proteins.
- Focused on studying protein interactions between herpesviruses and host cells.
Main Results:
- Successfully identified protein-protein interaction networks associated with herpesvirus infection.
- Demonstrated the efficacy of BioID coupled with LC-MS/MS in mapping complex biological interactions.
- Provided a foundation for understanding the molecular mechanisms of herpesvirus pathogenesis.
Conclusions:
- Proximity dependent biotinylation (BioID) is a powerful technique for identifying virus-host protein interactions.
- LC-MS/MS significantly enhances the discovery of protein networks.
- This approach offers a promising avenue for the development of targeted therapeutics against herpesviruses.
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