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Affinity Purification-Mass Spectroscopy Methods for Identifying Epstein-Barr Virus-Host Interactions.
- Source :
-
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2017; Vol. 1532, pp. 79-92. - Publication Year :
- 2017
-
Abstract
- Considerable insight into the function and mechanism of action of viral proteins has come from identifying the cellular proteins with which they interact. In recent years, mass spectrometry-based methods have emerged as the method of choice for protein interaction discovery due to their comprehensive and unbiased nature. Methods involving single affinity purifications of epitope-tagged viral proteins (AP-MS) and tandem affinity purifications of viral proteins with two purification tags (TAP tagging) have both been used to identify novel host interactions with EBV proteins. However, to date these methods have only been applied to a small number of EBV proteins. Here we provide detailed methods of AP-MS and TAP tagging approaches that can be applied to any EBV protein in order to discover its host interactions.
- Subjects :
- Chromatography, Affinity
Humans
Liquid-Liquid Extraction
Mass Spectrometry
Protein Binding
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Viral Proteins genetics
Viral Proteins metabolism
Epstein-Barr Virus Infections metabolism
Epstein-Barr Virus Infections virology
Herpesvirus 4, Human physiology
Host-Pathogen Interactions
Proteome
Proteomics methods
Subjects
Details
- Language :
- English
- ISSN :
- 1940-6029
- Volume :
- 1532
- Database :
- MEDLINE
- Journal :
- Methods in molecular biology (Clifton, N.J.)
- Publication Type :
- Academic Journal
- Accession number :
- 27873268
- Full Text :
- https://doi.org/10.1007/978-1-4939-6655-4_5