Establishment of a high-throughput screening assay for interaction inhibitor between BST-2 and Vpu / 病毒学报
Chinese Journal of Virology
;
(6): 633-638, 2012.
Article
in Chinese
| WPRIM
| ID: wpr-339993
ABSTRACT
BST-2 plays an important role in host innate immune response via inhibiting the release of HIV-1. HIV-1 accessory protein Vpu can interact with BST-2 through its transmembrane domains, degrade BST-2, and decrease BST-2 that are transported to the cell surface, thus anti-virus function of BST-2 is antagonized. In our study, we constructed plasmid RB connecting Rluc to the N-termimal of BST-2, and plasmid VE connecting EYFP to the C-terminal of Vpu. The two fusion proteins were co-expressed in 293 cells, and the interaction between the two proteins was detected via BRET method. And we further established a stable 293 cell line of dual-expression. By using BRET method, and the interaction between BST-2 and Vpu transmembrane domain as the target, a high-throughput screening assay was created that was expected to seek novel interaction inhibitors.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Protein Binding
/
Virology
/
Antigens, CD
/
HIV Infections
/
Cell Line
/
Chemistry
/
HIV-1
/
Protein Structure, Tertiary
/
Human Immunodeficiency Virus Proteins
/
Viral Regulatory and Accessory Proteins
Type of study:
Diagnostic study
/
Screening study
Limits:
Humans
Language:
Chinese
Journal:
Chinese Journal of Virology
Year:
2012
Type:
Article
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