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• W1895300367 abstract "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." @default.
• W1895300367 created "2016-06-24" @default.
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• W1895300367 date "2015-09-11" @default.
• W1895300367 modified "2023-10-15" @default.
• W1895300367 title "Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation" @default.
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• W1895300367 doi "https://doi.org/10.1186/s12985-015-0365-6" @default.
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