| Chapter title |
Affinity Purification-Mass Spectroscopy Methods for Identifying Epstein-Barr Virus-Host Interactions.
|
|---|---|
| Chapter number | 5 |
| Book title |
Epstein Barr Virus
|
| Published in |
Methods in molecular biology, January 2017
|
| DOI | 10.1007/978-1-4939-6655-4_5 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-6653-0, 978-1-4939-6655-4
|
| Authors |
Anna A. Georges, Lori Frappier |
| Editors |
Janos Minarovits, Hans Helmut Niller |
| 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. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 5 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Unspecified | 1 | 20% |
| Student > Master | 1 | 20% |
| Unknown | 3 | 60% |
| Readers by discipline | Count | As % |
|---|---|---|
| Unspecified | 1 | 20% |
| Agricultural and Biological Sciences | 1 | 20% |
| Unknown | 3 | 60% |