ArticleRetrovirology2005
Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates.
Article in Retrovirology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed.
- Real-Time Imaging of HIV-1 Protease Activation and Substrate Cleavage in Single Virions Assembling on the Plasma Membrane.Viruses · 2026Article
- Identifying Conserved Regions in HIV-1 Proteins by Entropy Analysis of Sequence Variability.International journal of molecular sciences · 2026Article
- High-throughput screening and characterization of novel inhibitors targeting HIV-1 protease precursor autoprocessing.Scientific reports · 2025Article
- Mechanism and Kinetics of HIV-1 Protease Activation.Viruses · 2024Review
- The conserved HIV-1 spacer peptide 2 triggers matrix lattice maturation.bioRxiv : the preprint server for biology · 2024Article
- The Assembly of HTLV-1-How Does It Differ from HIV-1?Viruses · 2024Review
- Interplay between protease and reverse transcriptase dimerization in a model HIV-1 polyprotein.Protein science : a publication of the Protein Society · 2024Article
- Molecular dynamics simulations of HIV-1 matrix-membrane interactions at different stages of viral maturation.Biophysical journal · 2024Article
- Modeling and Analysis of HIV-1 Pol Polyprotein as a Case Study for Predicting Large Polyprotein Structures.International journal of molecular sciences · 2024Article
- Article
- HIV-1 envelope facilitates the development of protease inhibitor resistance through acquiring mutations associated with viral entry and immune escape.Frontiers in microbiology · 2024Article
- HIV Infection: Shaping the Complex, Dynamic, and Interconnected Network of the Cytoskeleton.International journal of molecular sciences · 2023Review
- Cryo-EM structure of the HIV-1 Pol polyprotein provides insights into virion maturation.Science advances · 2022Article
- Inositol Hexakisphosphate (IP6) Accelerates Immature HIV-1 Gag Protein Assembly toward Kinetically Trapped Morphologies.Journal of the American Chemical Society · 2022Article
- Natural Immunity against HIV-1: Progression of Understanding after Association Studies.Viruses · 2022Review
- The HIV-1 Viral Protease Is Activated during Assembly and Budding Prior to Particle Release.Journal of virology · 2022Article
- Protease and gag diversity and drug resistance mutations among treatment-naive Mexican people living with HIV.BMC infectious diseases · 2022Article
- Effects of reduced gag cleavage efficiency on HIV-1 Gag-Pol package.BMC microbiology · 2022Article
- Advances in HIV-1 Assembly.Viruses · 2022Review
- Amino acid substitutions at the HIV-1 transframe region significantly impair virus infectivity.PloS one · 2022Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
We have examined the kinetics of processing of the HIV-1 Gag-Pro-Pol precursor in an in vitro assay with mature protease added in trans. The processing sites were cleaved at different rates to produce distinct intermediates. The initial cleavage occurred at the p2/NC site. Intermediate cleavages occurred at similar rates at the MA/CA and RT/IN sites, and to a lesser extent at sites upstream of RT. Late cleavages occurred at the sites flanking the protease (PR) domain, suggesting sequestering of these sites. We observed paired intermediates indicative of half- cleavage of RT/RH site, suggesting that the RT domain in Gag-Pro-Pol was in a dimeric form under these assay conditions. These results clarify our understanding of the processing kinetics of the Gag-Pro-Pol precursor and suggest regulated cleavage. Our results further suggest that early dimerization of the PR and RT domains may serve as a regulatory element to influence the kinetics of processing within the Pol domain.
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