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Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation
BACKGROUND: 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 antiretr...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4566291/ https://www.ncbi.nlm.nih.gov/pubmed/26362536 http://dx.doi.org/10.1186/s12985-015-0365-6 |
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author | Le Sage, Valerie Cinti, Alessandro Valiente-Echeverría, Fernando Mouland, Andrew J. |
author_facet | Le Sage, Valerie Cinti, Alessandro Valiente-Echeverría, Fernando Mouland, Andrew J. |
author_sort | Le Sage, Valerie |
collection | PubMed |
description | BACKGROUND: 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. FINDINGS: 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. CONCLUSIONS: 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12985-015-0365-6) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4566291 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-45662912015-09-12 Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation Le Sage, Valerie Cinti, Alessandro Valiente-Echeverría, Fernando Mouland, Andrew J. Virol J Short Report BACKGROUND: 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. FINDINGS: 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. CONCLUSIONS: 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12985-015-0365-6) contains supplementary material, which is available to authorized users. BioMed Central 2015-09-11 /pmc/articles/PMC4566291/ /pubmed/26362536 http://dx.doi.org/10.1186/s12985-015-0365-6 Text en © Le Sage et al. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Short Report Le Sage, Valerie Cinti, Alessandro Valiente-Echeverría, Fernando Mouland, Andrew J. Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation |
title | Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation |
title_full | Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation |
title_fullStr | Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation |
title_full_unstemmed | Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation |
title_short | Proteomic analysis of HIV-1 Gag interacting partners using proximity-dependent biotinylation |
title_sort | proteomic analysis of hiv-1 gag interacting partners using proximity-dependent biotinylation |
topic | Short Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4566291/ https://www.ncbi.nlm.nih.gov/pubmed/26362536 http://dx.doi.org/10.1186/s12985-015-0365-6 |
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