Specific inter-domain interactions stabilize a compact HIV-1 Gag conformation
نویسندگان
چکیده
منابع مشابه
Conformation of the HIV-1 Gag protein in solution.
A single multi-domain viral protein, termed Gag, is sufficient for assembly of retrovirus-like particles in mammalian cells. We have purified the human immunodeficiency virus type 1 (HIV-1) Gag protein (lacking myristate at its N terminus and the p6 domain at its C terminus) from bacteria. This protein is capable of assembly into virus-like particles in a defined in vitro system. We have report...
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The Gag protein of HIV multimerizes to form viral particles. The GagPol protein encoding virus-specific enzymes, such as protease, reverse transcriptase, and integrase, is incorporated into HIV particles via interactions with Gag. The catalytically active forms of these enzymes are dimeric or tetrameric. We employed Förster resonance energy transfer (FRET) assays to evaluate Gag-Gag, Gag-GagPol...
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HIVU53175 HIVCA9 U53175 422 bp gag Braaten, D. JVI 70, 4220 (1996) Comment: This study compared the five lineages of primate immunodeficiency viruses and found that only HIV-1 group M requires cyclophilin A for replication. HIV-1 gag binds to cyclophilin A and incorporates it into virions. If this process is disrupted, virion infectivity is inhibited. Cloned isolates from clades A, B, and D of ...
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One strategy to induce optimal cellular and humoral immune responses following immunization is to use vaccines or adjuvants that target dendritic cells and B cells. Activation of both cell types can be achieved using specific TLR ligands or agonists directed against their cognate receptor. In this study, we compared the ability of the TLR7/8 agonist R-848, which signals only via TLR7 in mice, w...
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ژورنال
عنوان ژورنال: PLOS ONE
سال: 2019
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0221256