Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation.
Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation.
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DOI：
10.1186/s12985-015-0365-6
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发表时间：
2015-09-11
期刊：
影响因子：
4.8
通讯作者：
Mouland AJ
中科院分区：
文献类型：
--
作者：
Le Sage V;Cinti A;Valiente-Echeverría F;Mouland AJ
The human immunodeficiency virus type 1 (HIV-1) Gag polyprotein is necessary and sufficient to assemble non-infectious particles. Given that HIV-1 subverts many host proteins at all stages of its life cycle, it is essential to identify these interactions as potential targets for antiretroviral therapy. This work demonstrates the use of proximity-dependent biotin identification (BioID) of host proteins and complexes that are proximal to the N-terminal domains of the HIV-1 Gag polyprotein. Two of the hits identified in the BioID screen were validated by immunoprecipation and confirmed the interaction of DDX17 and RPS6 with HIV-1 Gag. Our results show that BioID is both a successful and complementary method to screen for nearby interacting proteins of HIV-1 Gag during the replicative cycle in different cell lines. The online version of this article (doi:10.1186/s12985-015-0365-6) contains supplementary material, which is available to authorized users.
