| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10843151 | Protein Expression and Purification | 2013 | 7 Pages |
Abstract
Tetherin/BST-2/CD317 inhibits HIV-1 release from infected cells, while HIV-1 Vpu efficiently antagonizes tetherin based on intermolecular interactions between the transmembrane domains of each protein. In this study, we successfully partially purified His-tagged tetherin with a glycophosphatidylinositol deletion (delGPI) and His-tagged full-length Vpu from transiently transfected 293T cells using affinity chromatography. The in vitro interaction between these purified proteins was observed by a pull-down assay and ELISA. Detection of the Vpu/tetherin interaction by ELISA is a novel approach that would be advantageous for inhibitor screening in vitro. Successful co-purification of the tetherin/Vpu complex also provides a basis for further structural studies.
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Authors
Mingyu Lv, Yingzi Zhu, Jiawen Wang, Haihong Zhang, Xiaodan Wang, Tao Zuo, Donglai Liu, Jingyao Zhang, Jiaxin Wu, Wei Kong, Xianghui Yu,