ArticleJournal of virological methods2009
In vivo biotinylation and capture of HIV-1 matrix and integrase proteins.
Article in Journal of virological methods, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- An Enhanced Emtricitabine-Loaded Long-Acting Nanoformulation for Prevention or Treatment of HIV Infection.Antimicrobial agents and chemotherapy · 2017Article
- Article
- Cyclophilin B enhances HIV-1 infection.Virology · 2016Article
- Proteomics in the investigation of HIV-1 interactions with host proteins.Proteomics. Clinical applications · 2015Review
- Article
- Proteomic analysis of early HIV-1 nucleoprotein complexes.Journal of proteome research · 2013Article
- Article
- Replication of biotinylated human immunodeficiency viruses.Journal of virological methods · 2011Article
- Identification of host proteins associated with HIV-1 preintegration complexes isolated from infected CD4+ cells.Retrovirology · 2010Article
- Changes in the accessibility of the HIV-1 Integrase C-terminus in the presence of cellular proteins.Retrovirology · 2010Article
- Biochemical and virological analysis of the 18-residue C-terminal tail of HIV-1 integrase.Retrovirology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
This report describes the adaptation of the biotin ligase BirA-biotin acceptor sequence (BAS) labeling system to biotinylate specific human immunodeficiency virus 1 (HIV-1) proteins in vivo. Two HIV-1 clones were constructed, with the BAS introduced into the matrix region of gag or the integrase region of pol. Specific biotinylation of target proteins in virions was observed when molecular clones were co-expressed with BirA. Both BAS-containing viruses propagated in SupT1 T-cells although replication of the integrase clone was delayed. Further studies demonstrated that the integrase insertion yielded an approximate 40% reduction in single-round infectivity as assessed on MAGI-5 indicator cells, as well as in the in vitro integration activity of preintegration complexes extracted from acutely infected C8166-45 T-cells. Biotinylation of the integrase BAS tag furthermore rendered this virus non-infectious. The matrix viral clone by contrast displayed wild-type behavior under all conditions tested. These results therefore establish a system whereby biotinylated matrix protein in the context of replication-competent virus could be used to label and capture viral protein complexes in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.